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Protein Engineering vol. 1 no. 6 pp. 471-475, 1987
© 1987 Oxford University Press

OTHER

Three-dimensional structure of protein C inhibitor predicted from structure of {alpha}1-antitrypsin with computer graphics

K. Toma, S. Yamamoto1, Y. Deyashiki2 and K. Suzuki2

1Bio-Science Laboratory, Life Science Research Laboratories, Asahi Chemical Industry Fuji, Shizuoka 416 2Department of Laboratory Medicine, Mie University School of Medicine Tsu, Mie 514, Japan Computer Science Department, Life Science Research Laboratories, Asahi Chemical Industry Fuji, Shizuoka 416

The three-dimensional structure of a proteolytically modified protein C inhibitor, a member of the serine protease inhibitor superfamily, was constructed with computer graphics based on its amino acid sequence homology with that of the modified {alpha}1-antitrypsin whose structure had been elucidated by X-ray crystallography. The intact form of protein C inhibitor was predicted with an {alpha}-carbon model based on its hydrophilicity and hydrogen bond pattern. Furthermore, a model of its interaction with activated protein C was constructed based on the structure of the complex between trypsin and its inhibitor, which had been determined by X-ray crystallography.

Keywords: computer graphics/model building/protein C/protein C inhibitor/three-dimensional structure

Received August 28, 1987; revised November 25, 1987;
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