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From Proteopedia
Revision as of 08:52, 28 September 2014 by OCA (Talk | contribs)
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Mizuno H, Fujimoto Z, Atoda H, Morita T. Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X. Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7230-4. Epub 2001 Jun 12. PMID:11404471 doi:10.1073/pnas.131179698
