Lymphotoxin beta receptor

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Lymphotoxin beta receptor (TNFR superfamily, member 3)
Lymphotoxin b receptor.png
Crystallographic structure of a 24-residue peptide from the lymphotoxin-B receptor bound to TRAF3.[1]
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols LTBR ; CD18; D12S370; LT-BETA-R; TNF-R-III; TNFCR; TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3
External IDs OMIM600979 MGI104875 HomoloGene1753 ChEMBL: 1250360 GeneCards: LTBR Gene
RNA expression pattern
PBB GE LTBR 203005 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 4055 17000
Ensembl ENSG00000111321 ENSMUSG00000030339
UniProt P36941 P50284
RefSeq (mRNA) NM_001270987 NM_010736
RefSeq (protein) NP_001257916 NP_034866
Location (UCSC) Chr 12:
6.48 – 6.5 Mb
Chr 6:
125.31 – 125.31 Mb
PubMed search [1] [2]

Lymphotoxin beta receptor is a receptor for lymphotoxin which in humans is encoded by the LTBR gene.[2][3][4]

Function[edit]

The protein encoded by this gene is a member of the tumor necrosis factor (TNF) family of receptors. It is expressed on the surface of most cell types, including cells of epithelial and myeloid lineages, but not on T and B lymphocytes. The protein specifically binds the lymphotoxin membrane form (a complex of lymphotoxin-alpha and lymphtoxin-beta). The encoded protein and its ligand play a role in the development and organization of lymphoid tissue and transformed cells. Activation of the encoded protein can trigger apoptosis.[2]

Not only does the LTBR help trigger apoptosis, it can lead to the release of the cytokine interleukin 8. Overexpression of LTBR in HEK293 cells increases IL-8 promoter activity and leads to IL-8 release. LTBR is also essential for development and organization of the secondary lymphoid organs and chemokine release.[5]

Structure[edit]

The Ramachandran plots show that 64.6% of all residues were in a favored region. This structure was found using X-ray diffraction. The resolution is 3.50 angstroms. The alpha and beta angles are 90 degrees while the gamma angle is 120 degrees.[6]

Interactions[edit]

Lymphotoxin beta receptor has been shown to interact with Diablo homolog[7] and TRAF3.[8][9][10]

References[edit]

  1. ^ PDB 1RF3; Li C, Norris PS, Ni CZ, Havert ML, Chiong EM, Tran BR, Cabezas E, Reed JC, Satterthwait AC, Ware CF, Ely KR (December 2003). "Structurally distinct recognition motifs in lymphotoxin-beta receptor and CD40 for tumor necrosis factor receptor-associated factor (TRAF)-mediated signaling". J. Biol. Chem. 278 (50): 50523–9. doi:10.1074/jbc.M309381200. PMID 14517219. 
  2. ^ a b "Entrez Gene: LTBR lymphotoxin beta receptor (TNFR superfamily, member 3)". 
  3. ^ Baens M, Chaffanet M, Cassiman JJ, van den Berghe H, Marynen P (April 1993). "Construction and evaluation of a hncDNA library of human 12p transcribed sequences derived from a somatic cell hybrid". Genomics 16 (1): 214–8. doi:10.1006/geno.1993.1161. PMID 8486360. 
  4. ^ Crowe PD, VanArsdale TL, Walter BN, Ware CF, Hession C, Ehrenfels B, Browning JL, Din WS, Goodwin RG, Smith CA (April 1994). "A lymphotoxin-beta-specific receptor". Science 264 (5159): 707–10. doi:10.1126/science.8171323. PMID 8171323. 
  5. ^ Chang YH, Hsieh SL, Chen MC, Lin WW (August 2002). "Lymphotoxin beta receptor induces interleukin 8 gene expression via NF-kappaB and AP-1 activation". Exp. Cell Res. 278 (2): 166–74. doi:10.1006/excr.2002.5573. PMID 12169272. 
  6. ^ "MolProbity Ramachandran analysis". 
  7. ^ Kuai, Jun; Nickbarg Elliott; Wooters Joe; Qiu Yongchang; Wang Jack; Lin Lih-Ling (Apr 2003). "Endogenous association of TRAF2, TRAF3, cIAP1, and Smac with lymphotoxin beta receptor reveals a novel mechanism of apoptosis". J. Biol. Chem. (United States) 278 (16): 14363–9. doi:10.1074/jbc.M208672200. ISSN 0021-9258. PMID 12571250. 
  8. ^ VanArsdale, T L; VanArsdale S L; Force W R; Walter B N; Mosialos G; Kieff E; Reed J C; Ware C F (Mar 1997). "Lymphotoxin-beta receptor signaling complex: role of tumor necrosis factor receptor-associated factor 3 recruitment in cell death and activation of nuclear factor kappaB". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 94 (6): 2460–5. doi:10.1073/pnas.94.6.2460. ISSN 0027-8424. PMC 20110. PMID 9122217. 
  9. ^ Wu, M Y; Wang P Y; Han S H; Hsieh S L (Apr 1999). "The cytoplasmic domain of the lymphotoxin-beta receptor mediates cell death in HeLa cells". J. Biol. Chem. (UNITED STATES) 274 (17): 11868–73. doi:10.1074/jbc.274.17.11868. ISSN 0021-9258. PMID 10207006. 
  10. ^ Marsters, S A; Ayres T M; Skubatch M; Gray C L; Rothe M; Ashkenazi A (May 1997). "Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB and AP-1". J. Biol. Chem. (UNITED STATES) 272 (22): 14029–32. doi:10.1074/jbc.272.22.14029. ISSN 0021-9258. PMID 9162022. 

Further reading[edit]

External links[edit]