February 1, 2000Journal of Biological ChemistryOpen Access

Identification of Basic Residues in the Heparin-binding Exosite of Factor Xa Critical for Heparin and Factor Va Binding

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Population

Gla domainless forms of factor Xa (FXa) constructs

Design

Preclinical

Authors

ARAlireza R. RezaieUniversity of North Carolina at Chapel Hill

Discussion

Member takes

Implication

These heparin-binding residues warrant no clinical anticoagulation changes; leaves open their utility for exosite-targeted antithrombotics in human models.

Structured PICO

Population

Gla domainless forms of factor Xa (FXa) constructs

Intervention

Substitution of basic residues (Arg93, Lys96, Arg125, Arg165, Lys169, Lys236, and Arg240) with Ala

Outcome

Second-order association rate constant (k2) for inactivation by antithrombin and binding affinity to heparin-Sepharosesurrogate

Specific basic residues in the heparin-binding exosite of factor Xa, particularly Arg240 and Lys236, are critical for heparin binding, while Arg165 and Lys169 are key for factor Va and prothrombin recognition.

Cite This Study

Alireza R. Rezaie (2000) studied this question.

synapsesocial.com/papers/6a6fe16ffebe604dd708b490 https://doi.org/10.1074/jbc.275.5.3320

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Implication

These heparin-binding residues warrant no clinical anticoagulation changes; leaves open their utility for exosite-targeted antithrombotics in human models.