1cqp
From Proteopedia
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|PDB= 1cqp |SIZE=350|CAPTION= <scene name='initialview01'>1cqp</scene>, resolution 2.60Å | |PDB= 1cqp |SIZE=350|CAPTION= <scene name='initialview01'>1cqp</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=803:LOVASTATIN'>803</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1lfa|1LFA]], [[1zon|1ZON]], [[1zoo|1ZOO]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqp OCA], [http://www.ebi.ac.uk/pdbsum/1cqp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cqp RCSB]</span> | ||
}} | }} | ||
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[[Category: Weitz-Schmidt, G.]] | [[Category: Weitz-Schmidt, G.]] | ||
[[Category: Welzenbach, K.]] | [[Category: Welzenbach, K.]] | ||
| - | [[Category: 803]] | ||
| - | [[Category: MG]] | ||
[[Category: rossman fold]] | [[Category: rossman fold]] | ||
[[Category: structural basis for lfa-1 inhibition]] | [[Category: structural basis for lfa-1 inhibition]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:26:45 2008'' |
Revision as of 16:26, 30 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1LFA, 1ZON, 1ZOO
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX LFA-1 (CD11A) I-DOMAIN / LOVASTATIN AT 2.6 A RESOLUTION
Overview
The lymphocyte function-associated antigen (LFA-1) belongs to the family of beta2-integrins and plays an important role in T-cell activation and leukocyte migration to sites of inflammation. We report here that lovastatin, a drug clinically used for lowering cholesterol levels, inhibits the interaction of human LFA-1 with its counter-receptor intercellular adhesion molecule-1. Using nuclear magnetic resonance spectroscopy and X-ray crystallography we show that the inhibitor binds to a highly conserved domain of the LFA-1 alpha-chain called the I-domain. The first three-dimensional structure of an integrin inhibitor bound to its receptor reveals atomic details for a hitherto unknown mode of LFA-1 inhibition. It also sheds light into possible mechanisms of LFA-1 mediated signalling and will support the design of novel anti-adhesive and immunosuppressive drugs.
About this Structure
1CQP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11a I-domain., Kallen J, Welzenbach K, Ramage P, Geyl D, Kriwacki R, Legge G, Cottens S, Weitz-Schmidt G, Hommel U, J Mol Biol. 1999 Sep 10;292(1):1-9. PMID:10493852
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