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Integrin alpha L

From Wikipedia, the free encyclopedia
(Redirected fromCD11a)

Mammalian protein found in Homo sapiens
ITGAL
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

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,5E6U

Identifiers
AliasesITGAL, CD11A, LFA-1, LFA1A, integrin subunit alpha L
External IDsOMIM:153370;MGI:96606;HomoloGene:1666;GeneCards:ITGAL;OMA:ITGAL - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for ITGAL
Genomic location for ITGAL
Band16p11.2Start30,472,658bp[1]
End30,523,567bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for ITGAL
Genomic location for ITGAL
Band7 F3|7 69.44 cMStart126,895,432bp[2]
End126,934,310bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • granulocyte

  • monocyte

  • blood

  • spleen

  • lymph node

  • bone marrow cells

  • appendix

  • thymus

  • upper lobe of left lung

  • epithelium of colon
Top expressed in
  • granulocyte

  • thymus

  • mesenteric lymph nodes

  • blood

  • spleen

  • subcutaneous adipose tissue

  • submandibular gland

  • bone marrow

  • right lung lobe

  • stroma of bone marrow
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3683

16408

Ensembl

ENSG00000005844

ENSMUSG00000030830

UniProt

P20701

P24063

RefSeq (mRNA)

NM_001114380
NM_002209

NM_001253872
NM_001253873
NM_001253874
NM_008400

RefSeq (protein)

NP_001107852
NP_002200

NP_001240801
NP_001240802
NP_001240803
NP_032426

Location (UCSC)Chr 16: 30.47 – 30.52 MbChr 7: 126.9 – 126.93 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide), also known asITGAL, is a protein that in humans is encoded by theITGALgene.[5] CD11a functions in the immune system. It is involved in cellular adhesion and costimulatory signaling. It is the target of the drugefalizumab.

Function

[edit]

ITGAL gene 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 in 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.[6]

CD11a is one of the two components, along withCD18, which formlymphocyte function-associated antigen-1.

Efalizumab acts as animmunosuppressant by binding to CD11a but was withdrawn in 2009 because it was associated with severe side effects.

Interactions

[edit]

CD11a has been shown tointeract withICAM-1.[7][8][9]

See also

[edit]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000005844 –Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000030830 –Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^"NCBI".
  6. ^"Entrez Gene: ITGAL integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)".
  7. ^Lu C, Takagi J, Springer TA (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.276 (18):14642–8.doi:10.1074/jbc.M100600200.PMID 11279101.
  8. ^Shimaoka M, Xiao T, Liu JH, Yang Y, Dong Y, Jun CD, McCormack A, Zhang R, Joachimiak A, Takagi J, Wang JH, Springer TA (Jan 2003)."Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation".Cell.112 (1):99–111.doi:10.1016/S0092-8674(02)01257-6.PMC 4372089.PMID 12526797.
  9. ^Yusuf-Makagiansar H, Makagiansar IT, Hu Y, Siahaan TJ (Dec 2001). "Synergistic inhibitory activity of alpha- and beta-LFA-1 peptides on LFA-1/ICAM-1 interaction".Peptides.22 (12):1955–62.doi:10.1016/S0196-9781(01)00546-0.PMID 11786177.S2CID 54343441.

Further reading

[edit]
PDB gallery
  • 1cqp: CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX LFA-1 (CD11A) I-DOMAIN / LOVASTATIN AT 2.6 A RESOLUTION
    1cqp: CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX LFA-1 (CD11A) I-DOMAIN / LOVASTATIN AT 2.6 A RESOLUTION
  • 1dgq: NMR SOLUTION STRUCTURE OF THE INSERTED DOMAIN OF HUMAN LEUKOCYTE FUNCTION ASSOCIATED ANTIGEN-1
    1dgq: NMR SOLUTION STRUCTURE OF THE INSERTED DOMAIN OF HUMAN LEUKOCYTE FUNCTION ASSOCIATED ANTIGEN-1
  • 1lfa: CD11A I-DOMAIN WITH BOUND MN++
    1lfa: CD11A I-DOMAIN WITH BOUND MN++
  • 1mjn: Crystal Structure of the intermediate affinity aL I domain mutant
    1mjn: Crystal Structure of the intermediate affinity aL I domain mutant
  • 1mq8: Crystal structure of alphaL I domain in complex with ICAM-1
    1mq8: Crystal structure of alphaL I domain in complex with ICAM-1
  • 1mq9: Crystal structure of high affinity alphaL I domain with ligand mimetic crystal contact
    1mq9: Crystal structure of high affinity alphaL I domain with ligand mimetic crystal contact
  • 1mqa: Crystal structure of high affinity alphaL I domain in the absence of ligand or metal
    1mqa: Crystal structure of high affinity alphaL I domain in the absence of ligand or metal
  • 1rd4: An allosteric inhibitor of LFA-1 bound to its I-domain
    1rd4: An allosteric inhibitor of LFA-1 bound to its I-domain
  • 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
    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
  • 1xdd: X-ray structure of LFA-1 I-domain in complex with LFA703 at 2.2A resolution
    1xdd: X-ray structure of LFA-1 I-domain in complex with LFA703 at 2.2A resolution
  • 1xdg: X-ray structure of LFA-1 I-domain in complex with LFA878 at 2.1A resolution
    1xdg: X-ray structure of LFA-1 I-domain in complex with LFA878 at 2.1A resolution
  • 1xuo: X-ray structure of LFA-1 I-domain bound to a 1,4-diazepane-2,5-dione inhibitor at 1.8A resolution
    1xuo: X-ray structure of LFA-1 I-domain bound to a 1,4-diazepane-2,5-dione inhibitor at 1.8A resolution
  • 1zon: CD11A I-DOMAIN WITHOUT BOUND CATION
    1zon: CD11A I-DOMAIN WITHOUT BOUND CATION
  • 1zoo: CD11A I-DOMAIN WITH BOUND MAGNESIUM ION
    1zoo: CD11A I-DOMAIN WITH BOUND MAGNESIUM ION
  • 1zop: CD11A I-DOMAIN WITH BOUND MAGNESIUM ION
    1zop: CD11A I-DOMAIN WITH BOUND MAGNESIUM ION
  • 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
    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
  • 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
    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

External links

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101–150
151–200
201–250
251–300
301–350
Alpha
Beta
Dimers
Cytoadhesin receptor:
Fibrinogen receptor:
Fibronectin receptor:
Leukocyte-adhesion receptor:
Very late antigen receptor:
Vitronectin receptor:


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