Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen

Journal of Molecular Biology

Volumn 271, Issue 5, 1997, Pages 774-788

  Podobnik, Marjetka ^a   Kuhelj, Robert ^a   Turk, Vito ^a   Turk, Dušan ^a,b  

^a JO EF STEFAN INSTITUTE   (Slovenia)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Activation mechanism; Crystal structure; Cysteine protease; Procathepsin B; Zymogen

Indexed keywords

CARBOXYPEPTIDASE; CATHEPSIN B; CYSTEINE; CYSTEINE PROTEINASE; ENZYME PRECURSOR; THREONINE;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HUMAN; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN STRUCTURE;

EID: 0031554904     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1218     Document Type: Article

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