Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S

EMBO Journal

Volumn 18, Issue 4, 1999, Pages 793-803

  Gunčar, Gregor ^a   Pungerčič, Galina ^a   Klemenčič, Ivica ^a   Turk, Vito ^a   Turk, Dušan ^a  

^a JO EF STEFAN INSTITUTE   (Slovenia)

Author keywords

Cathepsin; Crystal structure; Invariant chain; MHC class II; Thyroglobulin type 1 domain

Indexed keywords

CATHEPSIN L; CATHEPSIN S; CYSTATIN; CYSTEINE PROTEINASE INHIBITOR; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; THYROGLOBULIN;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; DISULFIDE BOND; ENZYME ACTIVE SITE; EVOLUTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANTIGENS, DIFFERENTIATION, B-LYMPHOCYTE; BINDING SITES; CATHEPSINS; CRYSTALLOGRAPHY, X-RAY; CYSTEINE ENDOPEPTIDASES; ENDOPEPTIDASES; HISTOCOMPATIBILITY ANTIGENS CLASS II; HUMANS; KIDNEY; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEASE INHIBITORS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; THYROGLOBULIN;

EID: 0039547996     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.4.793     Document Type: Article

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