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Ruf W, Dickinson CD. Allosteric regulation of the cofactor-dependent serine protease coagulation factor VIIa. Trends Cardiovasc Med. 1998;8(8):350-6doi: 10.1016/s1050-1738(98)00031-0.
Ruf, W., & Dickinson, C. D. (1998). Allosteric regulation of the cofactor-dependent serine protease coagulation factor VIIa. Trends in cardiovascular medicine, 8(8), 350-6. https://doi.org/10.1016/s1050-1738(98)00031-0
Ruf, W, and Dickinson, C D. "Allosteric regulation of the cofactor-dependent serine protease coagulation factor VIIa." Trends in cardiovascular medicine vol. 8,8 (1998): 350-6. doi: https://doi.org/10.1016/s1050-1738(98)00031-0
Ruf W, Dickinson CD. Allosteric regulation of the cofactor-dependent serine protease coagulation factor VIIa. Trends Cardiovasc Med. 1998 Nov;8(8):350-6. doi: 10.1016/s1050-1738(98)00031-0. PMID: 14987549.
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Trends Cardiovasc Med. 1998 Nov;8(8):350-6. doi: 10.1016/s1050-1738(98)00031-0.

Allosteric regulation of the cofactor-dependent serine protease coagulation factor VIIa.

Trends in cardiovascular medicine

W Ruf, C D Dickinson

Affiliations

  1. Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA.

PMID: 14987549 DOI: 10.1016/s1050-1738(98)00031-0

Abstract

The integration of structure and function analysis of the tissue factor-factor VIIa complex has provided a detailed view of the functional surface of the extrinsic activation complex. An incomplete zymogen to enzyme transition is responsible for the strict cofactor dependence of catalytic function of factor VIIa. The mutational analysis demonstrates that factor VIIa is allosterically regulated by specific conformational linkages that involve the cofactor binding site, the catalytic cleft, and the macromolecular substrate exosite. Regions of the flexible activation domain appear to play an important role in the allosteric regulation of this cofactor-dependent coagulation serine protease.

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