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Possible structural implications of 20 mutations in the protein-C protease domain

Academic Article
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Overview

authors

  • Greengard, J. S.
  • Griffin, John
  • Fisher, C. L.

publication date

  • 1994

journal

  • Thrombosis and Haemostasis  Journal

abstract

  • 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.

subject areas

  • Epidermal Growth Factor
  • Models, Molecular
  • Point Mutation
  • Protein C
  • Protein C Deficiency
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Serine Endopeptidases
  • Solubility
  • Structure-Activity Relationship
  • Water
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Identity

International Standard Serial Number (ISSN)

  • 0340-6245

PubMed ID

  • 7740456
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Additional Document Info

start page

  • 869

end page

  • 873

volume

  • 72

issue

  • 6

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