Three-dimensional structure of protein C inhibitor predicted from structure of alpha 1-antitrypsin with computer graphics.
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.
Toma
K
K
Computer Science Department, Asahi Chemical Industry, Shizuoka, Japan.
Yamamoto
S
S
Deyashiki
Y
Y
Suzuki
K
K
D000595:Amino Acid Sequence; D001798:Blood Proteins; D003196:Computer Graphics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011480:Protease Inhibitors; D018046:Protein C Inhibitor; D011487:Protein Conformation; D000515:alpha 1-Antitrypsin
D001798:Blood Proteins; D011480:Protease Inhibitors; D018046:Protein C Inhibitor; D000515:alpha 1-Antitrypsin