The occluding loop in cathepsin B defines the pH dependence of inhibition by its propeptide

Biochemistry

Volumn 38, Issue 16, 1999, Pages 5017-5023

  Quraishi, Omar ^a   Nägler, Dorit K ^a,b   Fox, Ted ^b,d   Sivaraman, J ^b   Cygler, Miroslaw ^a,b   Mort, John S ^a,c   Storer, Andrew C ^a,b  

^a MCGILL UNIVERSITY   (Canada)

^b NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^c SHRINERS HOSPITAL FOR CHILDREN   (Canada)

^d VERTEX PHARMACEUTICALS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARTIC ACID; CATHEPSIN B; ENZYME PRECURSOR; HISTIDINE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING COMPETITION; BINDING KINETICS; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME DEGRADATION; ENZYME STABILITY; GENE DELETION; MOLECULAR MODEL; PH; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEINASE INHIBITION; SEQUENCE ANALYSIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; CATHEPSIN B; ENZYME PRECURSORS; ENZYME STABILITY; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, SECONDARY; RATS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0040909177     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi981950o     Document Type: Article

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