CD11a

4IXD, 1CQP, 1DGQ, 1LFA, 1MJN, 1MQ8, 1MQ9, 1MQA, 1RD4, 1T0P, 1XDD, 1XDG, 1XUO, 1ZON, 1ZOO, 1ZOP, 2ICA, 2K8O, 2M3E, 2O7N, 3BN3, 3BQM, 3BQN, 3E2M, 3EOA, 3EOB, 3F74, 3F78, 3HI6, 3M6F, 3TCX, 5E6S, 5E6R, 5E6U368316408ENSG00000005844ENSMUSG00000030830P20701P24063NM_001114380NM_002209NM_001253872NM_001253873NM_001253874NM_008400NP_001107852NP_002200NP_001240801NP_001240802NP_001240803NP_032426Integrin, 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.1cqp: CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX LFA-1 (CD11A) I-DOMAIN / LOVASTATIN AT 2.6 A RESOLUTION1dgq: NMR SOLUTION STRUCTURE OF THE INSERTED DOMAIN OF HUMAN LEUKOCYTE FUNCTION ASSOCIATED ANTIGEN-11lfa: CD11A I-DOMAIN WITH BOUND MN++1mjn: Crystal Structure of the intermediate affinity aL I domain mutant1mq8: Crystal structure of alphaL I domain in complex with ICAM-11mq9: Crystal structure of high affinity alphaL I domain with ligand mimetic crystal contact1mqa: Crystal structure of high affinity alphaL I domain in the absence of ligand or metal1rd4: An allosteric inhibitor of LFA-1 bound to its I-domain1t0p: Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A1xdd: X-ray structure of LFA-1 I-domain in complex with LFA703 at 2.2A resolution1xdg: X-ray structure of LFA-1 I-domain in complex with LFA878 at 2.1A resolution1xuo: X-ray structure of LFA-1 I-domain bound to a 1,4-diazepane-2,5-dione inhibitor at 1.8A resolution1zon: CD11A I-DOMAIN WITHOUT BOUND CATION1zoo: CD11A I-DOMAIN WITH BOUND MAGNESIUM ION1zop: CD11A I-DOMAIN WITH BOUND MAGNESIUM ION2ica: CD11a (LFA1) I-domain complexed with BMS-587101 aka 5-non-7-yl]methyl]-3-thiophenecarboxylicacid2o7n: CD11A (LFA1) I-domain complexed with 7A--6-(3,5-dichlorophenyl)-5-oxo-2,3,5,7A-tetrahydro-1H-pyrrolopyrrole-7-carbonitrile 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. 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 but was withdrawn in 2009 because it was associated with severe side effects. CD11a has been shown to interact with ICAM-1.