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- W2023297908 abstract "Significance Deletion of the flexible linker connecting the two kringles of prothrombin reduces the drastic enhancement of thrombin generation by cofactor Va from >3,000-fold observed with wild-type prothrombin to only 60-fold. The change proves that deletion of the linker mimics the effect of cofactor Va on prothrombin activation. The crystal structure of the deletion mutant reveals a contorted conformation where the domains are not vertically stacked, kringle-1 comes close to the protease domain, and the Gla-domain contacts kringle-2. These findings broaden our understanding of a key reaction of the blood coagulation cascade. Cofactor Va enhances activation of prothrombin by altering the architecture of the linker and inducing a conformation similar to the structure of the deletion mutant." @default.
- W2023297908 created "2016-06-24" @default.
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- W2023297908 date "2014-05-12" @default.
- W2023297908 modified "2023-10-11" @default.
- W2023297908 title "The linker connecting the two kringles plays a key role in prothrombin activation" @default.
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- W2023297908 doi "https://doi.org/10.1073/pnas.1403779111" @default.
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