What question did this study set out to answer?

Synthesize structural and biochemical evidence to explain how thrombin's multiple downstream functions are coordinated and directed during the hemostatic response.

July 1, 2005BloodOpen Access

Directing thrombin

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Authors

DLDavid A. LaneUniversity of California, Riverside HPHelen PhilippouUniversity of Leeds JHJames A. HuntingtonUniversity of Cambridge

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Implication

Narrative review demonstrates how cofactor competition for surface exosites directs thrombin activity during coagulation, indicating a key regulatory mechanism in hemostasis.

Key Points

Synthesize structural and biochemical evidence to explain how thrombin's multiple downstream functions are coordinated and directed during the hemostatic response.
Reviewed published structural findings from crystal structure analyses of thrombin and its macromolecular complexes.
Evaluated functional evidence from site-directed mutagenesis studies examining thrombin substrate and cofactor binding interfaces.
Structural analyses identify conserved active-site residues for substrate cleavage alongside overlapping surface binding regions termed exosites.
Competition among pathway-specific cofactors for these shared exosites serves as the primary mechanism governing thrombin's multifunctional substrate selection.

Cite This Study

Lane et al. (2005) studied this question.

synapsesocial.com/papers/6a8579aed06b31cc19d0c12f https://doi.org/10.1182/blood-2005-04-1710

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Implication

Narrative review demonstrates how cofactor competition for surface exosites directs thrombin activity during coagulation, indicating a key regulatory mechanism in hemostasis.

Directing thrombin

Discussion

Member takes

Implication

Key Points

Cite This Study

Directing thrombin

Discussion

Member takes

Implication

Key Points

Cite This Study

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