Possible Structural Implications of 20 Mutations in the Protein C Protease Domain

Judith S Greengard; John H Griffin; Cindy L Fisher

doi:10.1055/s-0038-1648976

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1994; 72(06): 869-873
DOI: 10.1055/s-0038-1648976

Original Article

Schattauer GmbH Stuttgart

Possible Structural Implications of 20 Mutations in the Protein C Protease Domain

Authors

Judith S Greengard

The Departments of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA, USA
John H Griffin

The Departments of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA, USA
Cindy L Fisher

The Departments of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA, USA

Abstract

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Summary

Analysis of naturally occurring protein mutations yields valuable insights into functionally important sequences. Characterizing mutations responsible for protein C deficiency at the molecular level has been the subject of intensive investigation. In a previous study, a three-dimensional model of the serine protease domain of protein C was used to analyze the set of protease domain mutations previously available. The mutations were largely found to fall into a limited number of categories. A recently updated protein C mutation data base has provided a number of new mutations which have been analyzed for structural predictions.

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References

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