What question did this study set out to answer?

To review the evolutionary and structural mechanisms through which natural exogenous and endogenous inhibitors exploit thrombin's active site and anion-binding exosites to suppress blood coagulation.

January 1, 2014Thrombosis and Haemostasis

Natural inhibitors of thrombin

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Authors

JHJames A. HuntingtonUniversity of Cambridge

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Implication

Review reveals structural mechanisms of endogenous serpins and exogenous inhibitors targeting thrombin exosites, highlighting evolutionary strategies to regulate blood coagulation.

Key Points

To review the evolutionary and structural mechanisms through which natural exogenous and endogenous inhibitors exploit thrombin's active site and anion-binding exosites to suppress blood coagulation.
Examined crystallographic data of exogenous thrombin inhibitors derived from the saliva of hematophagous organisms.
Analyzed structural models and complex-formation mechanics of the four endogenous human serpin inhibitors bound to thrombin.
Exogenous inhibitors from hematophagous animals employ diverse non-serpin peptide architectures to bind thrombin's active site cleft and exosites I and II.
Human endogenous regulation relies on four serpins that leverage exosite-dependent binding to disrupt thrombin's structural integrity, promoting cofactor release and clearance.

Cite This Study

James A. Huntington (2014) studied this question.

synapsesocial.com/papers/6a6f5f6d75498292b708c35e https://doi.org/10.1160/th13-10-0811

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Implication

Review reveals structural mechanisms of endogenous serpins and exogenous inhibitors targeting thrombin exosites, highlighting evolutionary strategies to regulate blood coagulation.

Natural inhibitors of thrombin

Discussion

Member takes

Implication

Key Points

Cite This Study

Natural inhibitors of thrombin

Discussion

Member takes

Implication

Key Points

Cite This Study

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