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A molecular model of the serine protease domain of activated protein C: application to the study of missense mutations causing protein C deficiency

Wacey, A. I., Pemberton, S., Cooper, David Neil, Kakkar, V. V. and Tuddenham, E. G. D. 1993. A molecular model of the serine protease domain of activated protein C: application to the study of missense mutations causing protein C deficiency. British Journal of Haematology 84 (2) , pp. 290-300. 10.1111/j.1365-2141.1993.tb03067.x

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Abstract

A molecular model of the serine protease domain of protein C was constructed by standard comparative methods. Individual missense mutations were inserted into the model and plausible explanations for their interference with protein C structure/function were derived through consideration of location, steric effects and protein stability. A hydrophilic cluster of many Arg and Lys residues, found adjacent to the active site cleft, is proposed to be involved in thrombomodulin and/or protein S interactions. Analysis of comparative binding studies also suggested the presence of an extended substrate binding pocket in the model.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Subjects: R Medicine > R Medicine (General)
Publisher: Wiley-Blackwell
ISSN: 0007-1048
Last Modified: 04 Jun 2017 06:33
URI: http://orca.cf.ac.uk/id/eprint/62016

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