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• W1985500018 startingPage "7164" @default.
• W1985500018 abstract "Thrombin-catalyzed activation of coagulation factor V (FV) is an essential positive feedback reaction within the blood clotting system. Efficient processing at the N- (Arg709-Ser710) and C-terminal activation cleavage sites (Arg1545-Ser1546) requires initial substrate interactions with 2 clusters of positively charged residues on the proteinase surface, exosites I and II. We addressed the mechanism of activation of human factor V (FV) using peptides that cover the entire acidic regions preceding these cleavage sites, FV (657-709)/ (FVa2) and FV(1481-1545)/(FVa3). FVa2 appears to interact mostly with exosite I, while both exosites are involved in interactions with the C-terminal linker. The 1.7-Å crystal structure of irreversibly inhibited thrombin bound to FVa2 unambiguously reveals docking of FV residues Glu666-Glu672 to exosite I. These findings were confirmed in a second, medium-resolution structure of FVa2 bound to the benzamidine-inhibited proteinase. Our results suggest that the acidic A2-B domain linker is involved in major interactions with thrombin during cofactor activation, with its more N-terminal hirudin-like sequence playing a critical role. Modeling experiments indicate that FVa2, and likely also FVa3, wrap around thrombin in productive thrombin·FV complexes that cover a large surface of the activator to engage the active site." @default.
• W1985500018 created "2016-06-24" @default.
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• W1985500018 date "2011-06-30" @default.
• W1985500018 modified "2023-10-18" @default.
• W1985500018 title "Structural basis of thrombin-mediated factor V activation: the Glu666-Glu672 sequence is critical for processing at the heavy chain–B domain junction" @default.
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• W1985500018 doi "https://doi.org/10.1182/blood-2010-10-315309" @default.
• W1985500018 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3143557" @default.
• W1985500018 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21555742" @default.
• W1985500018 hasPublicationYear "2011" @default.
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