CD11a
| Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide) |
PDB rendering based on 1cqp. |
| Available structures |
| PDB |
1CQP, 1DGQ, 1IJ4, 1LFA, 1MJN, 1MQ8, 1MQ9, 1MQA, 1RD4, 1T0P, 1XDD, 1XDG, 1XUO, 1ZON, 1ZOO, 1ZOP, 2ICA, 2K8O, 2O7N, 3BN3, 3BQM, 3BQN, 3E2M, 3EOA, 3EOB, 3F74, 3F78, 3HI6, 3M6F |
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| Identifiers |
| Symbols |
ITGAL; CD11A; LFA-1; LFA1A |
| External IDs |
OMIM: 153370 MGI: 96606 HomoloGene: 1666 GeneCards: ITGAL Gene |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
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| Entrez |
3683 |
16408 |
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| Ensembl |
ENSG00000005844 |
ENSMUSG00000030830 |
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| UniProt |
P20701 |
Q3T9N8 |
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| RefSeq (mRNA) |
NM_001114380.1 |
NM_008400.2 |
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| RefSeq (protein) |
NP_001107852.1 |
NP_032426.2 |
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| Location (UCSC) |
Chr 16:
30.48 – 30.53 Mb |
Chr 7:
134.44 – 134.48 Mb |
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| PubMed search |
[1] |
[2] |
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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
Interactions
CD11a has been shown to interact with ICAM-1.[2][3][4]
References
- ^ "Entrez Gene: ITGAL integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3683.
- ^ 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.
- ^ 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.
- ^ 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
- Lub M, van Kooyk Y, Figdor CG (1995). "Ins and outs of LFA-1.". Immunol. Today 16 (10): 479–83. doi:10.1016/0167-5699(95)80031-X. PMID 7576051.
- Dickeson SK, Santoro SA (1998). "Ligand recognition by the I domain-containing integrins.". Cell. Mol. Life Sci. 54 (6): 556–66. doi:10.1007/s000180050184. PMID 9676575.
- Porter JC, Hogg N (1999). "Integrins take partners: cross-talk between integrins and other membrane receptors.". Trends Cell Biol. 8 (10): 390–6. doi:10.1016/S0962-8924(98)01344-0. PMID 9789327.
- Giblin PA, Lemieux RM (2006). "LFA-1 as a key regulator of immune function: approaches toward the development of LFA-1-based therapeutics.". Curr. Pharm. Des. 12 (22): 2771–95. doi:10.2174/138161206777947731. PMID 16918410.
- Maurer D, Holter W, Majdic O, et al. (1991). "CD27 expression by a distinct subpopulation of human B lymphocytes.". Eur. J. Immunol. 20 (12): 2679–84. doi:10.1002/eji.1830201223. PMID 1702722.
- Kalter DC, Gendelman HE, Meltzer MS (1992). "Inhibition of human immunodeficiency virus infection in monocytes by monoclonal antibodies against leukocyte adhesion molecules.". Immunol. Lett. 30 (2): 219–27. doi:10.1016/0165-2478(91)90029-A. PMID 1757107.
- Alvarez V, Pulido R, Campanero MR, et al. (1992). "Differentially regulated cell surface expression of leukocyte adhesion receptors on neutrophils.". Kidney Int. 40 (5): 899–905. doi:10.1038/ki.1991.291. PMID 1762294.
- Valentin A, Lundin K, Patarroyo M, Asjö B (1990). "The leukocyte adhesion glycoprotein CD18 participates in HIV-1-induced syncytia formation in monocytoid and T cells.". J. Immunol. 144 (3): 934–7. PMID 1967280.
- Larson RS, Corbi AL, Berman L, Springer T (1989). "Primary structure of the leukocyte function-associated molecule-1 alpha subunit: an integrin with an embedded domain defining a protein superfamily". J. Cell Biol. 108 (2): 703–12. doi:10.1083/jcb.108.2.703. PMC 2115430. PMID 2537322. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2115430.
- Hildreth JE, Orentas RJ (1989). "Involvement of a leukocyte adhesion receptor (LFA-1) in HIV-induced syncytium formation". Science 244 (4908): 1075–8. doi:10.1126/science.2543075. PMID 2543075.
- Sanders ME, Makgoba MW, Sharrow SO, et al. (1988). "Human memory T lymphocytes express increased levels of three cell adhesion molecules (LFA-3, CD2, and LFA-1) and three other molecules (UCHL1, CDw29, and Pgp-1) and have enhanced IFN-gamma production". J. Immunol. 140 (5): 1401–7. PMID 2894392.
- Corbi AL, Larson RS, Kishimoto TK, et al. (1988). "Chromosomal location of the genes encoding the leukocyte adhesion receptors LFA-1, Mac-1 and p150,95. Identification of a gene cluster involved in cell adhesion". J. Exp. Med. 167 (5): 1597–607. doi:10.1084/jem.167.5.1597. PMC 2188934. PMID 3284962. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2188934.
- te Velde AA, Keizer GD, Figdor CG (1987). "Differential function of LFA-1 family molecules (CD11 and CD18) in adhesion of human monocytes to melanoma and endothelial cells". Immunology 61 (3): 261–7. PMC 1453405. PMID 3301632. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1453405.
- Qu A, Leahy DJ (1995). "Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin". Proc. Natl. Acad. Sci. U.S.A. 92 (22): 10277–81. doi:10.1073/pnas.92.22.10277. PMC 40779. PMID 7479767. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=40779.
- Turner ML, McIlwaine K, Anthony RS, Parker AC (1995). "Differential expression of cell adhesion molecules by human hematopoietic progenitor cells from bone marrow and mobilized adult peripheral blood". Stem Cells 13 (3): 311–6. doi:10.1002/stem.5530130312. PMID 7542116.
- Marzusch K, Ruck P, Geiselhart A, et al. (1993). "Distribution of cell adhesion molecules on CD56++, CD3-, CD16- large granular lymphocytes and endothelial cells in first-trimester human decidua". Hum. Reprod. 8 (8): 1203–8. PMID 7691868.
- Capobianchi MR, Ameglio F, Cordiali Fei P, et al. (1994). "Coordinate induction of interferon alpha and gamma by recombinant HIV-1 glycoprotein 120". AIDS Res. Hum. Retroviruses 9 (10): 957–62. doi:10.1089/aid.1993.9.957. PMID 7904170.
- Berman PW, Nakamura GR (1994). "Adhesion mediated by intercellular adhesion molecule 1 attenuates the potency of antibodies that block HIV-1 gp160-dependent syncytium formation". AIDS Res. Hum. Retroviruses 10 (5): 585–93. doi:10.1089/aid.1994.10.585. PMID 7917519.
- Chirmule N, Oyaizu N, Saxinger C, Pahwa S (1994). "Nef protein of HIV-1 has B-cell stimulatory activity". AIDS 8 (6): 733–4. doi:10.1097/00002030-199406000-00002. PMID 8086129.
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PDB gallery
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1cqp: CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX LFA-1 (CD11A) I-DOMAIN / LOVASTATIN AT 2.6 A RESOLUTION
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1dgq: NMR SOLUTION STRUCTURE OF THE INSERTED DOMAIN OF HUMAN LEUKOCYTE FUNCTION ASSOCIATED ANTIGEN-1
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1lfa: CD11A I-DOMAIN WITH BOUND MN++
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1mjn: Crystal Structure of the intermediate affinity aL I domain mutant
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1mq8: Crystal structure of alphaL I domain in complex with ICAM-1
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1mq9: Crystal structure of high affinity alphaL I domain with ligand mimetic crystal contact
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1mqa: Crystal structure of high affinity alphaL I domain in the absence of ligand or metal
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1rd4: An allosteric inhibitor of LFA-1 bound to its I-domain
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1t0p: Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A
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1xdd: X-ray structure of LFA-1 I-domain in complex with LFA703 at 2.2A resolution
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1xdg: X-ray structure of LFA-1 I-domain in complex with LFA878 at 2.1A resolution
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1xuo: X-ray structure of LFA-1 I-domain bound to a 1,4-diazepane-2,5-dione inhibitor at 1.8A resolution
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1zon: CD11A I-DOMAIN WITHOUT BOUND CATION
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1zoo: CD11A I-DOMAIN WITH BOUND MAGNESIUM ION
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1zop: CD11A I-DOMAIN WITH BOUND MAGNESIUM ION
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2ica: CD11a (LFA1) I-domain complexed with BMS-587101 aka 5-[(5S, 9R)-9-(4-cyanophenyl)-3-(3,5-dichlorophenyl)-1-methyl-2,4-dioxo-1,3,7-triazaspiro [4.4]non-7-yl]methyl]-3-thiophenecarboxylicacid
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2o7n: CD11A (LFA1) I-domain complexed with 7A-[(4-cyanophenyl)methyl]-6-(3,5-dichlorophenyl)-5-oxo-2,3,5,7A-tetrahydro-1H-pyrrolo[1,2-A]pyrrole-7-carbonitrile
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External links
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| 1-50 |
CD1 ( a-c, 1A, 1D, 1E) · CD2 · CD3 ( γ, δ, ε) · CD4 · CD5 · CD6 · CD7 · CD8 ( a) · CD9 · CD10 · CD11 (a, b, c) · CD13 · CD14 · CD15 · CD16 ( A, B) · CD18 · CD19 · CD20 · CD21 · CD22 · CD23 · CD24 · CD25 · CD26 · CD27 · CD28 · CD29 · CD30 · CD31 · CD32 ( A, B) · CD33 · CD34 · CD35 · CD36 · CD37 · CD38 · CD39 · CD40 · CD41 · CD42 ( a, b, c, d) · CD43 · CD44 · CD45 · CD46 · CD47 · CD48 · CD49 ( a, b, c, d, e, f) · CD50
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| 51-100 |
CD51 · CD52 · CD53 · CD54 · CD55 · CD56 · CD57 · CD58 · CD59 · CD61 · CD62 ( E, L, P) · CD63 · CD64 ( A, B, C) · CD66 ( a, b, c, d, e, f) · CD68 · CD69 · CD70 · CD71 · CD72 · CD73 · CD74 · CD78 · CD79 ( a, b) · CD80 · CD81 · CD82 · CD83 · CD84 · CD85 ( a, d, e, h, j, k) · CD86 · CD87 · CD88 · CD89 · CD90 · CD91- CD92 · CD93 · CD94 · CD95 · CD96 · CD97 · CD98 · CD99 · CD100
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| 101-150 |
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| 151-200 |
CD151 · CD152 · CD153 · CD154 · CD155 · CD156 ( a, b, c) · CD157 · CD158 ( a, d, e, i, k) · CD159 ( a, c) · CD160 · CD161 · CD162 · CD163 · CD164 · CD166 · CD167 ( a, b) · CD168 · CD169 · CD170 · CD171 · CD172 ( a, b, g) · CD174 · CD177 · CD178 · CD179 ( a, b) · CD181 · CD182 · CD183 · CD184 · CD185 · CD186 · CD191 · CD192 · CD193 · CD194 · CD195 · CD196 · CD197 · CDw198 · CDw199 · CD200
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| 201-250 |
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| 251-300 |
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| 301-350 |
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| Alpha |
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| Beta |
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| Dimers |
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see also cell surface receptor deficiencies
B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
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