CD11a

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Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)

PDB rendering based on 1cqp.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ITGAL ; CD11A; LFA-1; LFA1A
External IDs OMIM153370 MGI96606 HomoloGene1666 ChEMBL: 1803 GeneCards: ITGAL Gene
RNA expression pattern
PBB GE ITGAL 213475 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3683 16408
Ensembl ENSG00000005844 ENSMUSG00000030830
UniProt P20701 P24063
RefSeq (mRNA) NM_001114380 NM_001253872
RefSeq (protein) NP_001107852 NP_001240801
Location (UCSC) Chr 16:
30.48 – 30.53 Mb
Chr 7:
127.3 – 127.34 Mb
PubMed search [1] [2]

Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide), also known as ITGAL, is a human gene which functions in the immune system. It is involved in cellular adhesion and costimulatory signaling. It is the target of the drug efalizumab.

ITGAL encodes the integrin alpha L chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This I-domain containing alpha integrin combines with the beta 2 chain (ITGB2) to form the integrin lymphocyte function-associated antigen-1 (LFA-1), which is expressed on all leukocytes. LFA-1 plays a central role in leukocyte intercellular adhesion through interactions with its ligands, ICAMs 1-3 (intercellular adhesion molecules 1 through 3), and also functions in lymphocyte costimulatory signaling.[1]

CD11a is one of the two components, along with CD18, which form lymphocyte function-associated antigen-1.

Efalizumab acts as an immunosuppressant by binding to CD11a.

See also[edit]

Interactions[edit]

CD11a has been shown to interact with ICAM-1.[2][3][4]

References[edit]

  1. ^ "Entrez Gene: ITGAL integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)". 
  2. ^ Lu, C; Takagi J, Springer T A (May 2001). "Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state". J. Biol. Chem. (United States) 276 (18): 14642–8. doi:10.1074/jbc.M100600200. ISSN 0021-9258. PMID 11279101. 
  3. ^ Shimaoka, Motomu; Xiao Tsan, Liu Jin-Huan, Yang Yuting, Dong Yicheng, Jun Chang-Duk, McCormack Alison, Zhang Rongguang, Joachimiak Andrzej, Takagi Junichi, Wang Jia-Huai, Springer Timothy A (Jan 2003). "Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation". Cell (United States) 112 (1): 99–111. doi:10.1016/S0092-8674(02)01257-6. ISSN 0092-8674. PMID 12526797. 
  4. ^ Yusuf-Makagiansar, H; Makagiansar I T, Hu Y, Siahaan T J (Dec 2001). "Synergistic inhibitory activity of alpha- and beta-LFA-1 peptides on LFA-1/ICAM-1 interaction". Peptides (United States) 22 (12): 1955–62. doi:10.1016/S0196-9781(01)00546-0. ISSN 0196-9781. PMID 11786177. 

Further reading[edit]

External links[edit]