Thermodynamic linkage between the S1 site, the Na+ site, and the Ca2+ site in the protease domain of human activated protein C (APC). Sodium ion in the APC crystal structure is coordinated to four carbonyl groups from two separate loops.

The Journal of biological chemistry

Volumn 277, Issue 32, 2002, Pages 28987-28995

  Schmidt, Amy E ^a   Padmanabhan, Kaillathe ^a   Underwood, Matthew C ^a   Bode, Wolfram ^a   Mather, Timothy ^a   Bajaj, S Paul ^a  

^a SAINT LOUIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBENZOIC ACID; BLOOD CLOTTING FACTOR 10A; CALCIUM; HYDROGEN; ION; LEUCINE; NUCLEASE S1; PROTEIN C; SERINE; SODIUM; THROMBIN; TRYPTOPHAN; VALINE;

ARTICLE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; ENZYME SPECIFICITY; HUMAN; HYDROLYSIS; KINETICS; METABOLISM; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

4-AMINOBENZOIC ACID; ASPERGILLUS NUCLEASE S1; CALCIUM; CRYSTALLOGRAPHY, X-RAY; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FACTOR XA; HUMANS; HYDROGEN; HYDROLYSIS; IONS; KINETICS; LEUCINE; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN C; PROTEIN STRUCTURE, TERTIARY; SERINE; SODIUM; SUBSTRATE SPECIFICITY; THERMODYNAMICS; THROMBIN; TRYPTOPHAN; VALINE;

EID: 0037047347     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M201892200     Document Type: Article

References (0)