1czt
From Proteopedia
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| - | [[Image:1czt.gif|left|200px]] | + | [[Image:1czt.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V''' | + | {{Structure |
| + | |PDB= 1czt |SIZE=350|CAPTION= <scene name='initialview01'>1czt</scene>, resolution 1.87Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CZT is a [ | + | 1CZT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CZT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10586886 10586886] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: membrane-binding]] | [[Category: membrane-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:30:55 2008'' |
Revision as of 08:30, 20 March 2008
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CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V
Contents |
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.
Disease
Known diseases associated with this structure: Budd-Chiari syndrome OMIM:[227400], Hemorrhagic diathesis due to factor V deficiency OMIM:[227400], Thromboembolism susceptibility due to factor V Leiden OMIM:[227400], Thrombophilia due to factor V Liverpool OMIM:[227400]
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
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