The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation

EMBO Journal

Volumn 22, Issue 17, 2003, Pages 4356-4364

  Förster, Andreas ^a   Whitby, Frank G ^a   Hill, Christopher P ^a  

^a UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

Author keywords

7 Fold symmetry; Activation; Macromolecular crystal structure; Multisubunit complex; Proteasome

Indexed keywords

20S PROTEASOME; ASPARTIC ACID; PROLINE; PROTEASOME; PROTEASOME 11S ACTIVATOR PROTEIN; PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

7 FOLD SYMMETRIC PORE CONFORMATION; ARCHAEBACTERIUM; ARTICLE; CLUSTER ANALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; EUKARYOTE; EVOLUTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN INTERACTION; STRUCTURE ANALYSIS; THERMOPLASMA ACIDOPHILUM; YEAST;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; CYSTEINE ENDOPEPTIDASES; ENDOPEPTIDASES; EVOLUTION, MOLECULAR; HUMANS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID; THERMOPLASMA;

ARCHAEA; EUKARYOTA; THERMOPLASMA ACIDOPHILUM;

EID: 0043192299     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg436     Document Type: Article

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