2r7e
From Proteopedia
Crystal Structure Analysis of Coagulation Factor VIII
Overview
Factor VIII (fVIII) is a serum protein in the coagulation cascade that nucleates the assembly of a membrane-bound protease complex on the surface of activated platelets at the site of a vascular injury. Hemophilia A is caused by a variety of mutations in the factor VIII gene and typically requires replacement therapy with purified protein. We have determined the structure of a fully active, recombinant form of factor VIII (r-fVIII), which consists of a heterodimer of peptides, respectively containing the A1-A2 and A3-C1-C2 domains. The structure permits unambiguous modeling of the relative orientations of the 5 domains of r-fVIII. Comparison of the structures of fVIII, fV, and ceruloplasmin indicates that the location of bound metal ions and of glycosylation, both of which are critical for domain stabilization and association, overlap at some positions but have diverged at others.
About this Structure
2R7E is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The tertiary structure and domain organization of coagulation factor VIII., Shen BW, Spiegel PC, Chang CH, Huh JW, Lee JS, Kim J, Kim YH, Stoddard BL, Blood. 2008 Feb 1;111(3):1240-7. Epub 2007 Oct 26. PMID:17965321 Page seeded by OCA on Wed Apr 16 23:05:51 2008
Categories: Homo sapiens | Protein complex | Shen, B W. | Stoddard, B L. | Acute phase | Blood clotting | Blood coagulation | C2 domain fold | Calcium | Ceruloplasmin fold | Cupper protein fold | Disease mutation | Glycoprotein | Hemophilia | Metal-binding | Pharmaceutical | Polymorphism | Secreted | Sulfation
