1cqp: Difference between revisions

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New page: left|200px<br /> <applet load="1cqp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cqp, resolution 2.60Å" /> '''CRYSTAL STRUCTURE A...
 
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[[Image:1cqp.gif|left|200px]]<br />
[[Image:1cqp.jpg|left|200px]]<br /><applet load="1cqp" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1cqp" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1cqp, resolution 2.60&Aring;" />
caption="1cqp, resolution 2.60&Aring;" />
'''CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX LFA-1 (CD11A) I-DOMAIN / LOVASTATIN AT 2.6 A RESOLUTION'''<br />
'''CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX LFA-1 (CD11A) I-DOMAIN / LOVASTATIN AT 2.6 A RESOLUTION'''<br />
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==About this Structure==
==About this Structure==
1CQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and 803 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CQP OCA].  
1CQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=803:'>803</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQP OCA].  


==Reference==
==Reference==
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[[Category: structural basis for lfa-1 inhibition]]
[[Category: structural basis for lfa-1 inhibition]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:24:31 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:36:45 2008''

Revision as of 13:36, 15 February 2008

File:1cqp.jpg


1cqp, resolution 2.60Å

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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 with MG and 803 as ligands. 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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