β2 microglobulin also known as B2M is a component of MHC class I molecules, which are present on all nucleated cells (excludes red blood cells).[1][2] In humans, the β2 microglobulin protein[3] is encoded by the B2M gene.[2][4]
[edit] Structure and function
Schematic representation of MHC class I
β2 microglobulin lies lateral to the α3 chain on the cell surface. Unlike α3, β2 has no transmembrane region. Directly above β2 (i.e. away from the cell) lies the α1 chain, which itself is lateral to the α2.
β2 microglobulin associates not only with the alpha chain of MHC class I molecules, but also with class I-like molecules such as CD1 and Qa[disambiguation needed 
].
An additional function is association with the HFE protein, together regulating endocytosis of iron into intestinal cells. Loss of this function causes iron excess and hemochromatosis.
[edit] Clinical significance
In patients on long-term hemodialysis, it can aggregate into amyloid fibers that deposit in joint spaces, a disease known as dialysis-related amyloidosis.
Mice models deficient for the β2 microglobulin gene have been engineered. These mice demonstrate that β2 microglobulin is necessary for cell surface expression of MHC class I and stability of the peptide binding groove. In fact, in the absence of β2 microglobulin, very limited amounts of MHC class I (classical and non-classical) molecules can be detected on the surface. In the absence of MHC class I, CD8 T cells cannot develop. (CD8 T cells are a subset of T cells involved in the development of acquired immunity.) Low levels of β2 microglobulin can indicate non-progression of HIV.
Levels of beta-2 microglobulin can be elevated in multiple myeloma and lymphoma, though in these cases primary amyloidosis (amyloid light chain) and secondary amyloidosis (Amyloid associated protein) are more common. The normal value of beta-2 microglobulin is <0.2 mg/dL.[5] However, with respect to multiple myeloma, the levels of beta2-microglobulin may also be at the other end of the spectrum. Diagnostic testing for multiple myeloma includes obtaining the beta2-microglobulin level, for this level is an important prognostic indicator. A patient with a level <0.004 g/L is expected to have a median survival of 43 months, while one with a level >0.004 g/L has a median survival of only 12 months.[6]
[edit] References
- ^ "Entrez Gene: Beta-2-microglobulin". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=567.
- ^ a b Güssow D, Rein R, Ginjaar I, Hochstenbach F, Seemann G, Kottman A, Ploegh HL (1 November 1987). "The human beta 2-microglobulin gene. Primary structure and definition of the transcriptional unit". J. Immunol. 139 (9): 3132–8. PMID 3312414. http://www.jimmunol.org/cgi/content/abstract/139/9/3132.
- ^ Cunningham BA, Wang JL, Berggård I, Peterson PA (November 1973). "The complete amino acid sequence of beta 2-microglobulin". Biochemistry 12 (24): 4811–22. doi:10.1021/bi00748a001. PMID 4586824.
- ^ Suggs SV, Wallace RB, Hirose T, Kawashima EH, Itakura K (November 1981). "Use of synthetic oligonucleotides as hybridization probes: isolation of cloned cDNA sequences for human beta 2-microglobulin". Proc. Natl. Acad. Sci. U.S.A. 78 (11): 6613–7. doi:10.1073/pnas.78.11.6613. PMC 349099. PMID 6171820. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=349099.
- ^ Pignone M, Nicoll D; McPhee SJ (2004). Pocket guide to diagnostic tests (4th ed.). New York: McGraw-Hill. pp. 191. ISBN 0-07-141184-4.
- ^ Munshi NC, Longo DL, Anderson KC (2011). "Chapter 111: Plasma Cell Disorders". In Loscalzo J, Longo DL, Fauci AS, Dennis LK, Hauser SL. Harrison's Principles of Internal Medicine (18th ed.). McGraw-Hill Professional. pp. 936–44. ISBN 0-07-174889-X.
[edit] Further reading
- Huang WC, Havel JJ, Zhau HE, Qian WP, Lue HW, Chu CY, Nomura T, Chung LW. (2008). "β2-Microglobulin Signaling Blockade Inhibited Androgen Receptor Axis and Caused Apoptosis in Human Prostate Cancer Cells". Clin. Cancer Res. 14 (17): 5341–7. doi:10.1158/1078-0432.CCR-08-0793. PMC 3032570. PMID 18765525. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3032570.
- Huang WC, Wu D, Xie Z, Zhau HE, Nomura T, Zayzafoon M, Pohl J, Hsieh CL, Weitzmann MN, Farach-Carson MC, Chung LW. (2006). "Beta2-microglobulin is a signaling and growth-promoting factor for human prostate cancer bone metastasis". Cancer Res. 66 (18): 9108–16. doi:10.1158/0008-5472.CAN-06-1996. PMID 16982753.
- Winchester JF, Salsberg JA, Levin NW (2004). "Beta-2 microglobulin in ESRD: an in-depth review". Advances in renal replacement therapy 10 (4): 279–309. doi:10.1053/j.arrt.2003.11.003. PMID 14681859.
- Krangel MS, Orr HT, Strominger JL (1980). "Assembly and maturation of HLA-A and HLA-B antigens in vivo". Cell 18 (4): 979–91. doi:10.1016/0092-8674(79)90210-1. PMID 93026.
- Okon M, Bray P, Vucelić D (1992). "1H NMR assignments and secondary structure of human beta 2-microglobulin in solution". Biochemistry 31 (37): 8906–15. doi:10.1021/bi00152a030. PMID 1390678.
- Guo HC, Jardetzky TS, Garrett TP et al (1992). "Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle". Nature 360 (6402): 364–6. doi:10.1038/360364a0. PMID 1448153.
- Gattoni-Celli S, Kirsch K, Timpane R, Isselbacher KJ (1992). "Beta 2-microglobulin gene is mutated in a human colon cancer cell line (HCT) deficient in the expression of HLA class I antigens on the cell surface". Cancer Res. 52 (5): 1201–4. PMID 1737380.
- Saper MA, Bjorkman PJ, Wiley DC (1991). "Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution". J. Mol. Biol. 219 (2): 277–319. doi:10.1016/0022-2836(91)90567-P. PMID 2038058.
- Caruana RJ, Lobel SA, Leffell MS et al (1991). "Tumor necrosis factor, interleukin-1 and beta 2-microglobulin levels in chronic hemodialysis patients". The International journal of artificial organs 13 (12): 794–8. PMID 2289831.
- Connors LH, Shirahama T, Skinner M et al (1985). "In vitro formation of amyloid fibrils from intact beta 2-microglobulin". Biochem. Biophys. Res. Commun. 131 (3): 1063–8. doi:10.1016/0006-291X(85)90198-6. PMID 2413854.
- Hochman JH, Shimizu Y, DeMars R, Edidin M (1988). "Specific associations of fluorescent beta-2-microglobulin with cell surfaces. The affinity of different H-2 and HLA antigens for beta-2-microglobulin". J. Immunol. 140 (7): 2322–9. PMID 2450918.
- Homma N, Gejyo F, Isemura M, Arakawa M (1989). "Collagen-binding affinity of beta-2-microglobulin, a preprotein of hemodialysis-associated amyloidosis". Nephron 53 (1): 37–40. doi:10.1159/000185699. PMID 2674742.
- Bataille R, Grenier J, Commes T (1988). "In vitro production of beta 2 microglobulin by human myeloma cells". Cancer Invest. 6 (3): 271–7. doi:10.3109/07357908809080649. PMID 3048575.
- Hönig R, Marsen T, Schad S et al (1989). "Correlation of beta-2-microglobulin concentration changes to changes of distribution volume". The International journal of artificial organs 11 (6): 459–64. PMID 3060434.
- Bjorkman PJ, Saper MA, Samraoui B et al (1987). "Structure of the human class I histocompatibility antigen, HLA-A2". Nature 329 (6139): 506–12. doi:10.1038/329506a0. PMID 3309677.
- Güssow D, Rein R, Ginjaar I et al (1987). "The human beta 2-microglobulin gene. Primary structure and definition of the transcriptional unit". J. Immunol. 139 (9): 3132–8. PMID 3312414.
- Cunningham BA, Wang JL, Berggård I, Peterson PA (1974). "The complete amino acid sequence of beta 2-microglobulin". Biochemistry 12 (24): 4811–22. doi:10.1021/bi00748a001. PMID 4586824.
- Suggs SV, Wallace RB, Hirose T et al (1982). "Use of synthetic oligonucleotides as hybridization probes: isolation of cloned cDNA sequences for human beta 2-microglobulin". Proc. Natl. Acad. Sci. U.S.A. 78 (11): 6613–7. doi:10.1073/pnas.78.11.6613. PMC 349099. PMID 6171820. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=349099.
- Momoi T, Suzuki M, Titani K et al (1995). "Amino acid sequence of a modified beta 2-microglobulin in renal failure patient urine and long-term dialysis patient blood". Clin. Chim. Acta 236 (2): 135–44. doi:10.1016/0009-8981(95)06039-G. PMID 7554280.
- Collins EJ, Garboczi DN, Karpusas MN, Wiley DC (1995). "The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain". Proc. Natl. Acad. Sci. U.S.A. 92 (4): 1218–21. doi:10.1073/pnas.92.4.1218. PMC 42670. PMID 7862664. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=42670.
- Matoba R, Okubo K, Hori N et al (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene 146 (2): 199–207. doi:10.1016/0378-1119(94)90293-3. PMID 8076819.
- Wang Z, Cao Y, Albino AP et al (1993). "Lack of HLA class I antigen expression by melanoma cells SK-MEL-33 caused by a reading frameshift in beta 2-microglobulin messenger RNA". J. Clin. Invest. 91 (2): 684–92. doi:10.1172/JCI116249. PMC 288010. PMID 8432869. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=288010.
[edit] External links
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PDB gallery
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1a1m: MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2
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1a1n: MHC CLASS I MOLECULE B*3501 COMPLEXED WITH PEPTIDE VPLRPMTY FROM THE NEF PROTEIN (75-82) OF HIV1
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1a1o: MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE LS6 (KPIVQYDNF) FROM THE MALARIA PARASITE P. FALCIPARUM
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1a6z: HFE (HUMAN) HEMOCHROMATOSIS PROTEIN
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1a9b: DECAMER-LIKE CONFORMATION OF A NANO-PEPTIDE BOUND TO HLA-B3501 DUE TO NONSTANDARD POSITIONING OF THE C-TERMINUS
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1a9e: DECAMER-LIKE CONFORMATION OF A NANO-PEPTIDE BOUND TO HLA-B3501 DUE TO NONSTANDARD POSITIONING OF THE C-TERMINUS
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1agb: ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGRKKYKL-3R MUTATION)
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1agc: ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKKYQL-7Q MUTATION)
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1agd: ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKKYKL-INDEX PEPTIDE)
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1age: ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKKYRL-7R MUTATION)
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1agf: ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKRYKL-5R MUTATION)
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1akj: COMPLEX OF THE HUMAN MHC CLASS I GLYCOPROTEIN HLA-A2 AND THE T CELL CORECEPTOR CD8
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1ao7: COMPLEX BETWEEN HUMAN T-CELL RECEPTOR, VIRAL PEPTIDE (TAX), AND HLA-A 0201
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1b0g: CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A2.1)/BETA 2-MICROGLOBULIN/PEPTIDE P1049 COMPLEX
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1b0r: CRYSTAL STRUCTURE OF HLA-A*0201 COMPLEXED WITH A PEPTIDE WITH THE CARBOXYL-TERMINAL GROUP SUBSTITUTED BY A METHYL GROUP
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1bd2: COMPLEX BETWEEN HUMAN T-CELL RECEPTOR B7, VIRAL PEPTIDE (TAX) AND MHC CLASS I MOLECULE HLA-A 0201
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1c16: CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/DELTA T CELL LIGAND T22
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1ce6: MHC CLASS I H-2DB COMPLEXED WITH A SENDAI VIRUS NUCLEOPROTEIN PEPTIDE
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1cg9: COMPLEX RECOGNITION OF THE SUPERTYPIC BW6-DETERMINANT ON HLA-B AND-C MOLECULES BY THE MONOCLONAL ANTIBODY SFR8-B6
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1de4: HEMOCHROMATOSIS PROTEIN HFE COMPLEXED WITH TRANSFERRIN RECEPTOR
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1duy: CRYSTAL STRUCTURE OF HLA-A*0201/OCTAMERIC TAX PEPTIDE COMPLEX
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1duz: HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A 0201) IN COMPLEX WITH A NONAMERIC PEPTIDE FROM HTLV-1 TAX PROTEIN
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1e27: NONSTANDARD PEPTIDE BINDING OF HLA-B*5101 COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM1(LPPVVAKEI)
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1e28: NONSTANDARD PEPTIDE BINDING OF HLA-B*5101 COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM2(TAFTIPSI)
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1eey: Crystal Structure Determination Of HLA A2 Complexed to Peptide GP2 with the substitution (I2L/V5L/L9V)
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1eez: Crystal Structure Determination of HLA-A2.1 Complexed to GP2 Peptide Variant(I2L/V5L)
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1efx: STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3
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1exu: CRYSTAL STRUCTURE OF THE HUMAN MHC-RELATED FC RECEPTOR
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1gzp: CD1B IN COMPLEX WITH GM2 GANGLIOSIDE
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1gzq: CD1B IN COMPLEX WITH PHOPHATIDYLINOSITOL
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1hhg: THE ANTIGENIC IDENTITY OF PEPTIDE(SLASH)MHC COMPLEXES: A COMPARISON OF THE CONFORMATION OF FIVE PEPTIDES PRESENTED BY HLA-A2
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1hhh: THE ANTIGENIC IDENTITY OF PEPTIDE(SLASH)MHC COMPLEXES: A COMPARISON OF THE CONFORMATION OF FIVE PEPTIDES PRESENTED BY HLA-A2
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1hhi: THE ANTIGENIC IDENTITY OF PEPTIDE(SLASH)MHC COMPLEXES: A COMPARISON OF THE CONFORMATION OF FIVE PEPTIDES PRESENTED BY HLA-A2
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1hhj: THE ANTIGENIC IDENTITY OF PEPTIDE(SLASH)MHC COMPLEXES: A COMPARISON OF THE CONFORMATION OF FIVE PEPTIDES PRESENTED BY HLA-A2
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1hhk: THE ANTIGENIC IDENTITY OF PEPTIDE(SLASH)MHC COMPLEXES: A COMPARISON OF THE CONFORMATION OF FIVE PEPTIDES PRESENTED BY HLA-A2
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1hsa: THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC
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1hsb: DIFFERENT LENGTH PEPTIDES BIND TO HLA-AW68 SIMILARLY AT THEIR ENDS BUT BULGE OUT IN THE MIDDLE
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1i1f: CRYSTAL STRUCTURE OF HUMAN CLASS I MHC (HLA-A2.1) COMPLEXED WITH BETA 2-MICROGLOBULIN AND HIV-RT VARIANT PEPTIDE I1Y
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1i1y: CRYSTAL STRUCTURE OF HUMAN CLASS I MHC (HLA-A2.1) COMPLEXED WITH BETA 2-MICROGLOBULIN AND HIV-RT VARIANT PEPTIDE I1Y
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1i4f: CRYSTAL STRUCTURE OF HLA-A*0201/MAGE-A4-PEPTIDE COMPLEX
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1i7r: CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1058
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1i7t: CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-5V
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1i7u: CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-6V
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1im3: Crystal Structure of the human cytomegalovirus protein US2 bound to the MHC class I molecule HLA-A2/tax
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1im9: Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1 bound to its MHC ligand HLA-Cw4
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1jf1: Crystal structure of HLA-A2*0201 in complex with a decameric altered peptide ligand from the MART-1/Melan-A
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1jgd: HLA-B*2709 bound to deca-peptide s10R
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1jge: HLA-B*2705 bound to nona-peptide m9
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1jht: Crystal structure of HLA-A2*0201 in complex with a nonameric altered peptide ligand (ALGIGILTV) from the MART-1/Melan-A.
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1jnj: NMR solution structure of the human beta2-microglobulin
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1k5n: HLA-B*2709 BOUND TO NONA-PEPTIDE M9
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1kpr: The human non-classical major histocompatibility complex molecule HLA-E
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1ktl: The human non-classical major histocompatibility complex molecule HLA-E
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1lds: Crystal Structure of monomeric human beta-2-microglobulin
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1lp9: Xenoreactive complex AHIII 12.2 TCR bound to p1049/HLA-A2.1
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1m05: HLA B8 in complex with an Epstein Barr Virus determinant
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1m6o: Crystal Structure of HLA B*4402 in complex with HLA DPA*0201 peptide
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1mhe: THE HUMAN NON-CLASSICAL MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE HLA-E
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1mi5: The crystal structure of LC13 TcR in complex with HLAB8-EBV peptide complex
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1n2r: A natural selected dimorphism in HLA B*44 alters self, peptide reportoire and T cell recognition.
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1of2: CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)
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1oga: A STRUCTURAL BASIS FOR IMMUNODOMINANT HUMAN T-CELL RECEPTOR RECOGNITION.
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1ogt: CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)
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1onq: Crystal Structure of CD1a in Complex with a Sulfatide
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1p7q: Crystal Structure of HLA-A2 Bound to LIR-1, a Host and Viral MHC Receptor
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1py4: Beta2 microglobulin mutant H31Y displays hints for amyloid formations
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1q94: Structures of HLA-A*1101 in complex with immunodominant nonamer and decamer HIV-1 epitopes clearly reveal the presence of a middle anchor residue
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1qew: HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A 0201) COMPLEX WITH A NONAMERIC PEPTIDE FROM MELANOMA-ASSOCIATED ANTIGEN 3 (RESIDUES 271-279)
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1qlf: MHC CLASS I H-2DB COMPLEXED WITH GLYCOPEPTIDE K3G
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1qqd: CRYSTAL STRUCTURE OF HLA-CW4, A LIGAND FOR THE KIR2D NATURAL KILLER CELL INHIBITORY RECEPTOR
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1qr1: POOR BINDING OF A HER-2/NEU EPITOPE (GP2) TO HLA-A2.1 IS DUE TO A LACK OF INTERACTIONS IN THE CENTER OF THE PEPTIDE
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1qrn: CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2 BOUND TO ALTERED HTLV-1 TAX PEPTIDE P6A
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1qse: STRUCTURE OF HUMAN A6-TCR BOUND TO HLA-A2 COMPLEXED WITH ALTERED HTLV-1 TAX PEPTIDE V7R
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1qsf: STRUCTURE OF A6-TCR BOUND TO HLA-A2 COMPLEXED WITH ALTERED HTLV-1 TAX PEPTIDE Y8A
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1qvo: STRUCTURES OF HLA-A*1101 IN COMPLEX WITH IMMUNODOMINANT NONAMER AND DECAMER HIV-1 EPITOPES CLEARLY REVEAL THE PRESENCE OF A MIDDLE ANCHOR RESIDUE
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1r3h: Crystal Structure of T10
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1s8d: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-3A
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1s9w: Crystal Structure Analysis of NY-ESO-1 epitope, SLLMWITQC, in complex with HLA-A2
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1s9x: Crystal Structure Analysis of NY-ESO-1 epitope analogue, SLLMWITQA, in complex with HLA-A2
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1s9y: Crystal Structure Analysis of NY-ESO-1 epitope analogue, SLLMWITQS, in complex with HLA-A2
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1sys: Crystal structure of HLA, B*4403, and peptide EEPTVIKKY
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1syv: HLA-B*4405 complexed to the dominant self ligand EEFGRAYGF
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1t1w: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-3F6I8V
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1t1x: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-4L
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1t1y: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-5V
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1t1z: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-6A
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1t20: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-6I
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1t21: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9, monoclinic crystal
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1t22: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9, orthorhombic crystal
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1tmc: THE THREE-DIMENSIONAL STRUCTURE OF A CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE MISSING THE ALPHA3 DOMAIN OF THE HEAVY CHAIN
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1tvb: Crystal structure of Melanoma Antigen gp100(209-217) Bound to Human Class I MHC HLA-A2
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1tvh: Crystal structure of Modified Melanoma Antigen gp100(209-T2M) Bound to Human Class I MHC HLA-A2
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1uqs: THE CRYSTAL STRUCTURE OF HUMAN CD1B WITH A BOUND BACTERIAL GLYCOLIPID
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1uxs: CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE (LMP2)OF EPSTEIN-BARR VIRUS
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1uxw: CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE (LMP2) OF EPSTEIN-BARR VIRUS
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1vgk: The crystal structure of class I Major histocompatibility complex, H-2Kd at 2.0 A resolution
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1w0v: CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE SELF-PEPTIDE TIS FROM EGF-RESPONSE FACTOR 1
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1w0w: CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED WITH THE SELF-PEPTIDE TIS FROM EGF-RESPONSE FACTOR 1
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1w72: CRYSTAL STRUCTURE OF HLA-A1:MAGE-A1 IN COMPLEX WITH FAB-HYB3
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1x7q: Crystal structure of HLA-A*1101 with sars nucleocapsid peptide
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