What question did this study set out to answer?

To elucidate the molecular mechanism of prothrombin processing by prothrombinase through structural investigation.

April 24, 2026The EMBO JournalOpen Access

Prothrombinase processivity is conferred by substrate allostery

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Structural analysis uncovers how substrate allostery aids prothrombin processing by prothrombinase, offering new insights.

To elucidate the molecular mechanism of prothrombin processing by prothrombinase through structural investigation.
Cryo-electron microscopy (cryo-EM) was utilized to visualize prothrombinase bound to prothrombin and meizothrombin.
Three-dimensional structural data was analyzed to understand enzyme-substrate interactions.
Two cryo-EM structures of prothrombinase observed, highlighting key interactions between fVa and prothrombin.
A conformational change after cleavage at Arg320 was identified, altering interactions and facilitating the second cleavage site presentation.
Substrate allostery was introduced as a new mechanism influencing enzymatic activity.

Üstok et al. (2026) studied this question.

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