1cqp: Difference between revisions

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[[Image:1cqp.~~jpg~~|left|200px]]

[[Image:1cqp.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX LFA-1 (CD11A) I-DOMAIN / LOVASTATIN AT 2.6 A RESOLUTION~~'''~~

===CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX LFA-1 (CD11A) I-DOMAIN / LOVASTATIN AT 2.6 A RESOLUTION===

~~==Overview==~~

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10493852}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10493852 is the PubMed ID number.

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==About this Structure==

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[[Category: Rossman fold]]

[[Category: Structural basis for lfa-1 inhibition]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:00:53 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:09:13 2008''

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-[[Image:1cqp.jpg|left|200px]]
+{{Seed}}
+[[Image:1cqp.png|left|200px]]
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 {{STRUCTURE_1cqp|  PDB=1cqp  |  SCENE=  }}
-'''CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX LFA-1 (CD11A) I-DOMAIN / LOVASTATIN AT 2.6 A RESOLUTION'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10493852}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10493852 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10493852}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Rossman fold]]
 [[Category: Structural basis for lfa-1 inhibition]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:00:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:09:13 2008''