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• W2037876981 endingPage "7234" @default.
• W2037876981 startingPage "7230" @default.
• W2037876981 abstract "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." @default.
• W2037876981 created "2016-06-24" @default.
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• W2037876981 creator A5058488316 @default.
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• W2037876981 date "2001-06-12" @default.
• W2037876981 modified "2023-10-03" @default.
• W2037876981 title "Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X" @default.
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• W2037876981 doi "https://doi.org/10.1073/pnas.131179698" @default.
• W2037876981 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/34651" @default.
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