1iod
CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE COAGULATION FACTOR X BINDING PROTEIN FROM SNAKE VENOM AND THE GLA DOMAIN OF FACTOR X
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OverviewOverview
The gamma-carboxyglutamic acid (Gla) domain of blood coagulation factors, is responsible for Ca2+-dependent phospholipid membrane binding. Factor, X-binding protein (X-bp), an anticoagulant protein from snake venom, specifically binds to the Gla domain of factor X. The crystal structure of, X-bp in complex with the Gla domain peptide of factor X at 2.3-A, resolution showed that the anticoagulation is based on the fact that two, patches of the Gla domain essential for membrane binding are buried in the, complex formation. The Gla domain thus is expected to be a new target of, anticoagulant drugs, and X-bp provides a basis for designing them. This, structure also provides a membrane-bound model of factor X.
About this StructureAbout this Structure
1IOD is a Single protein structure of sequence from Bos taurus and Deinagkistrodon acutus with CA as ligand. The following page contains interesting information on the relation of 1IOD with [Tissue Factor]. Active as Coagulation factor Xa, with EC number 3.4.21.6 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X., Mizuno H, Fujimoto Z, Atoda H, Morita T, Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7230-4. Epub 2001 Jun 12. PMID:11404471
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