The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site

Structure

Volumn 12, Issue 6, 2004, Pages 1087-1097

  Harris, Seth F ^a   Shiau, Andrew K ^a   Agard, David A ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 90; MONOMER; PROTEIN; PROTEIN HTPG; SOLVENT; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HYDROLYSIS; KINETICS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 2942533020     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2004.03.020     Document Type: Article

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