The crystal structure of a Cys25 → Ala mutant of human procathepsin S elucidates enzyme-prosequence interactions

Protein Science

Volumn 15, Issue 11, 2006, Pages 2619-2629

  Kaulmann, Guido ^a,b,e,f   Palm, Gottfried J ^b,c   Schilling, Klaus ^a   Hilgenfeld, Rolf ^b,d   Wiederanders, Bernd ^a  

^a JENA UNIVERSITY HOSPITAL   (Germany)

^b FRITZ LIPMANN INSTITUTE   (Germany)

^c UNIVERSITY OF GREIFSWALD   (Germany)

^d UNIVERSITY OF LÜBECK   (Germany)

^e KAROLINSKA UNIVERSITY HOSPITAL   (Sweden)

^f BIOSCIENCLIP ^*  (Germany)

Author keywords

Crystal structure; Cysteine proteinase; Procathepsin S; Propeptide

Indexed keywords

ALANINE; CATHEPSIN S; CYSTEINE; ENZYME PRECURSOR;

AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ARTICLE; BACULOVIRUS; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME STRUCTURE; HYDROGEN BOND; LIGAND BINDING; MOLECULAR INTERACTION; MOLECULAR MODEL; MUTAGENESIS; MUTATION; NONHUMAN; PRIORITY JOURNAL; R FACTOR;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; CATHEPSINS; CRYSTALLOGRAPHY, X-RAY; ENZYME PRECURSORS; HUMANS; MODELS, MOLECULAR; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY;

RUMEX;

EID: 33751103711     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062401806     Document Type: Article

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