Possible structural implications of 20 mutations in the protein C protease domain.
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.
Greengard
J S
JS
Department of Molecular, Scripps Research Institute, La Jolla, CA 92037.
Griffin
J H
JH
Fisher
C L
CL
D004815:Epidermal Growth Factor / Q000737:chemistry; D008958:Models, Molecular; D017354:Point Mutation; D011486:Protein C / Q000737:chemistry*; D020151:Protein C Deficiency; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012697:Serine Endopeptidases / Q000737:chemistry*; D012995:Solubility; D013329:Structure-Activity Relationship; D014867:Water / Q000737:chemistry
D011486:Protein C; D014867:Water; D004815:Epidermal Growth Factor; D012697:Serine Endopeptidases