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rdf:type |
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lifeskim:mentions |
umls-concept:C0005456,
umls-concept:C0014834,
umls-concept:C0035647,
umls-concept:C0243044,
umls-concept:C0376525,
umls-concept:C0444626,
umls-concept:C1514562,
umls-concept:C1710236,
umls-concept:C1825534,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
6
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pubmed:dateCreated |
2004-7-27
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pubmed:databankReference |
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pubmed:abstractText |
Hsp90 is a ubiquitous, well-conserved molecular chaperone involved in the folding and stabilization of diverse proteins. Beyond its capacity for general protein folding, Hsp90 influences a wide array of cellular signaling pathways that underlie key biological and disease processes. It has been proposed that Hsp90 functions as a molecular clamp, dimerizing through its carboxy-terminal domain and utilizing ATP binding and hydrolysis to drive large conformational changes including transient dimerization of the amino-terminal and middle domains. We have determined the 2.6 A X-ray crystal structure of the carboxy-terminal domain of htpG, the Escherichia coli Hsp90. This structure reveals a novel fold and that dimerization is dependent upon the formation of a four-helix bundle. Remarkably, proximal to the helical dimerization motif, each monomer projects a short helix into solvent. The location, flexibility, and amphipathic character of this helix suggests that it may play a role in substrate binding and hence chaperone activity.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1087-97
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15274928-Adenosine Triphosphate,
pubmed-meshheading:15274928-Amino Acid Motifs,
pubmed-meshheading:15274928-Amino Acid Sequence,
pubmed-meshheading:15274928-Bacterial Proteins,
pubmed-meshheading:15274928-Binding Sites,
pubmed-meshheading:15274928-Crystallography, X-Ray,
pubmed-meshheading:15274928-Dimerization,
pubmed-meshheading:15274928-Dose-Response Relationship, Drug,
pubmed-meshheading:15274928-Escherichia coli,
pubmed-meshheading:15274928-Escherichia coli Proteins,
pubmed-meshheading:15274928-HSP90 Heat-Shock Proteins,
pubmed-meshheading:15274928-Hydrolysis,
pubmed-meshheading:15274928-Kinetics,
pubmed-meshheading:15274928-Models, Biological,
pubmed-meshheading:15274928-Models, Molecular,
pubmed-meshheading:15274928-Molecular Sequence Data,
pubmed-meshheading:15274928-Mutation,
pubmed-meshheading:15274928-Protein Binding,
pubmed-meshheading:15274928-Protein Conformation,
pubmed-meshheading:15274928-Protein Folding,
pubmed-meshheading:15274928-Protein Structure, Secondary,
pubmed-meshheading:15274928-Protein Structure, Tertiary,
pubmed-meshheading:15274928-Sequence Homology, Amino Acid
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pubmed:year |
2004
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pubmed:articleTitle |
The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site.
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pubmed:affiliation |
Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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