1fv4

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THREE DIMENSIONAL MODEL OF COAGULATION FACTOR VA

spinqualitylabelsall models 1fv4 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed A complete molecular model of blood coagulation factor Va (FVa) bound to anticoagulant activated protein C (APC) and to a phospholipid membrane was constructed. The three homologous A domains and the two homologous C domains of FVA were modeled based on the X-ray crystallographic structures of ceruloplasmin and C2 domain of factor V, respectively. The final arrangement of the five domains in the complete FVa model bound to a membrane incorporated extensive published experimental data. FVa binds the phospholipid membrane through its C2 domain while the A-domain trimer is located from 40 through 100 A above the membrane plane. From our model we infer a probable role for metal ions at the interface between FVa light and heavy chains, provide an explanation for the slower APC cleavage at Arg306 relative to Arg506, and predict specific interactions between positively and negatively charged exosites in APC and FVa, respectively. Three-dimensional model of coagulation factor Va bound to activated protein C.,Pellequer JL, Gale AJ, Getzoff ED, Griffin JH Thromb Haemost. 2000 Nov;84(5):849-57. PMID:11127867 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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