Engineering an anion-binding cavity in antichymotrypsin modulates the 'spring-loaded' serpin-protease interaction

Biochemistry

Volumn 37, Issue 10, 1998, Pages 3297-3304

  Lukacs, Christine M ^a   Rubin, Harvey ^a   Christianson, David W ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; ANION; CHYMOTRYPSIN INHIBITOR; SERINE PROTEINASE INHIBITOR; SODIUM CHLORIDE;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME INHIBITOR INTERACTION; ENZYME KINETICS; ENZYME MODIFICATION; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; THERMODYNAMICS;

ANIONS; BASE SEQUENCE; BINDING SITES; CHYMOTRYPSIN; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; HUMANS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SERPINS; THERMODYNAMICS;

EID: 0032502262     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi972359e     Document Type: Article

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