1czt: Difference between revisions

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[[Image:1czt.gif|left|200px]]
[[Image:1czt.gif|left|200px]]


{{Structure
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{{STRUCTURE_1czt|  PDB=1czt |  SCENE= }}  
|RELATEDENTRY=[[1czs|1CZS]], [[1czv|1CZV]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1czt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1czt OCA], [http://www.ebi.ac.uk/pdbsum/1czt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1czt RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V'''
'''CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V'''
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[[Category: Kane, W H.]]
[[Category: Kane, W H.]]
[[Category: Macedo-Ribeiro, S.]]
[[Category: Macedo-Ribeiro, S.]]
[[Category: blood clotting]]
[[Category: Blood clotting]]
[[Category: calcium-independent]]
[[Category: Calcium-independent]]
[[Category: coagulation]]
[[Category: Coagulation]]
[[Category: discoidin family]]
[[Category: Discoidin family]]
[[Category: membrane-binding]]
[[Category: Membrane-binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:17:14 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:31:41 2008''

Revision as of 10:17, 2 May 2008

File:1czt.gif

Template:STRUCTURE 1czt

CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V


Overview

Rapid and controlled clot formation is achieved through sequential activation of circulating serine proteinase precursors on phosphatidylserine-rich procoagulant membranes of activated platelets and endothelial cells. The homologous complexes Xase and prothrombinase, each consisting of an active proteinase and a non-enzymatic cofactor, perform critical steps within this coagulation cascade. The activated cofactors VIIIa and Va, highly specific for their cognate proteinases, are each derived from precursors with the same A1-A2-B-A3-C1-C2 architecture. Membrane binding is mediated by the C2 domains of both cofactors. Here we report two crystal structures of the C2 domain of human factor Va. The conserved beta-barrel framework provides a scaffold for three protruding loops, one of which adopts markedly different conformations in the two crystal forms. We propose a mechanism of calcium-independent, stereospecific binding of factors Va and VIIIa to phospholipid membranes, on the basis of (1) immersion of hydrophobic residues at the apices of these loops in the apolar membrane core; (2) specific interactions with phosphatidylserine head groups in the groove enclosed by these loops; and (3) favourable electrostatic contacts of basic side chains with negatively charged membrane phosphate groups.

About this Structure

1CZT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structures of the membrane-binding C2 domain of human coagulation factor V., Macedo-Ribeiro S, Bode W, Huber R, Quinn-Allen MA, Kim SW, Ortel TL, Bourenkov GP, Bartunik HD, Stubbs MT, Kane WH, Fuentes-Prior P, Nature. 1999 Nov 25;402(6760):434-9. PMID:10586886 Page seeded by OCA on Fri May 2 13:17:14 2008

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