The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L

FEBS Letters

Volumn 576, Issue 3, 2004, Pages 358-362

  Soukenik, Michael ^a,d   Diehl, Anne ^a,b   Leidert, Martina ^a   Sievert, Volker ^b,c   Büssow, Konrad ^b,c   Leitner, Dietmar ^a,b   Labudde, Dirk ^a,b   Ball, Linda J ^a   Lechner, Annette ^e   Nägler, Dorit K ^e   Oschkinat, Hartmut ^a,d  

^a LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

^b Proteinstrukturfabrik   (Germany)

^c MAX PLANCK INSTITUTE FOR MOLECULAR GENETICS   (Germany)

^d FREIE UNIVERSITÄT BERLIN   (Germany)

^e UNIVERSITY OF MUNICH   (Germany)

Author keywords

Cathepsin L; NMR; p47; p97; Protein structure; SEP

Indexed keywords

AMINO ACID; CATHEPSIN L; CYSTEINE PROTEINASE; PROTEIN P47;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; CATHEPSIN B; CATHEPSINS; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; DNA PRIMERS; HUMANS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 6344287938     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.09.037     Document Type: Article

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