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 ORCID: https://orcid.org/0000-0002-8943-8484, 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:	27 Oct 2022 08:20
URI:	https://orca.cardiff.ac.uk/id/eprint/62016

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