1d7p: Difference between revisions

Revision as of 22:38, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1d7p.png

Template:STRUCTURE 1d7p

Crystal structure of the c2 domain of human factor viii at 1.5 a resolution at 1.5 ACrystal structure of the c2 domain of human factor viii at 1.5 a resolution at 1.5 A

Template:ABSTRACT PUBMED 10586887

About this StructureAbout this Structure

1D7P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the C2 domain of human factor VIII at 1.5 A resolution., Pratt KP, Shen BW, Takeshima K, Davie EW, Fujikawa K, Stoddard BL, Nature. 1999 Nov 25;402(6760):439-42. PMID:10586887

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OCA

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-'''Crystal structure of the c2 domain of human factor viii at 1.5 a resolution at 1.5 A'''
+===Crystal structure of the c2 domain of human factor viii at 1.5 a resolution at 1.5 A===
-==Overview==
+<!--
-Human factor VIII is a plasma glycoprotein that has a critical role in blood coagulation. Factor VIII circulates as a complex with von Willebrand factor. After cleavage by thrombin, factor VIIIa associates with factor IXa at the surface of activated platelets or endothelial cells. This complex activates factor X (refs 6, 7), which in turn converts prothrombin to thrombin in the presence of factor Va (refs 8, 9). The carboxyl-terminal C2 domain of factor VIII contains sites that are essential for its binding to von Willebrand factor and to negatively charged phospholipid surfaces. Here we report the structure of human factor VIII C2 domain at 1.5 A resolution. The structure reveals a beta-sandwich core, from which two beta-turns and a loop display a group of solvent-exposed hydrophobic residues. Behind the hydrophobic surface lies a ring of positively charged residues. This motif suggests a mechanism for membrane binding involving both hydrophobic and electrostatic interactions. The structure explains, in part, mutations in the C2 region of factor VIII that lead to bleeding disorders in haemophilia A.
+The line below this paragraph, {{ABSTRACT_PUBMED_10586887}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10586887 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10586887}}
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 [[Category: Beta sandwich]]
 [[Category: Blood clotting]]
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