1lqv: Difference between revisions

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[[Image:1lqv.jpg|left|200px]]
{{Seed}}
[[Image:1lqv.png|left|200px]]


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{{STRUCTURE_1lqv|  PDB=1lqv  |  SCENE=  }}  
{{STRUCTURE_1lqv|  PDB=1lqv  |  SCENE=  }}  


'''Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C.'''
===Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C.===




==Overview==
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The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus. Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses. To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C. The structures were strikingly similar to CD1d. A tightly bound phospholipid resides in the groove typically involved in antigen presentation. The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain. Extraction of the lipid resulted in loss of protein C binding, which could be restored by lipid reconstitution. CD1d augments the immune response by presenting glycolipid antigens. The EPCR structure is a model for how CD1d binds lipids and further suggests additional potential functions for EPCR in immune regulation, possibly including the anti-phospholipid syndrome.
The line below this paragraph, {{ABSTRACT_PUBMED_12034704}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12034704}}


==About this Structure==
==About this Structure==
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[[Category: Ca ion binding]]
[[Category: Ca ion binding]]
[[Category: Phospholipid binding groove]]
[[Category: Phospholipid binding groove]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:11:27 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:49:36 2008''

Revision as of 18:49, 2 July 2008

File:1lqv.png

Template:STRUCTURE 1lqv

Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C.

Template:ABSTRACT PUBMED 12034704

About this Structure

1LQV is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of the endothelial protein C receptor and a bound phospholipid., Oganesyan V, Oganesyan N, Terzyan S, Qu D, Dauter Z, Esmon NL, Esmon CT, J Biol Chem. 2002 Jul 12;277(28):24851-4. Epub 2002 May 28. PMID:12034704

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