| Structural basis of interdomain communication in the Hsc70 chaperone. | |
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MedLine Citation:
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PMID: 16307916 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Hsp70 family proteins are highly conserved chaperones involved in protein folding, degradation, targeting and translocation, and protein complex remodeling. They are comprised of an N-terminal nucleotide binding domain (NBD) and a C-terminal protein substrate binding domain (SBD). ATP binding to the NBD alters SBD conformation and substrate binding kinetics, but an understanding of the mechanism of interdomain communication has been hampered by the lack of a crystal structure of an intact chaperone. We report here the 2.6 angstroms structure of a functionally intact bovine Hsc70 (bHsc70) and a mutational analysis of the observed interdomain interface and the immediately adjacent interdomain linker. This analysis identifies interdomain interactions critical for chaperone function and supports an allosteric mechanism in which the interdomain linker invades and disrupts the interdomain interface when ATP binds. |
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Authors:
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Jianwen Jiang; Kondury Prasad; Eileen M Lafer; Rui Sousa |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Molecular cell Volume: 20 ISSN: 1097-2765 ISO Abbreviation: Mol. Cell Publication Date: 2005 Nov |
Date Detail:
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Created Date: 2005-11-25 Completed Date: 2006-01-05 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 9802571 Medline TA: Mol Cell Country: United States |
Other Details:
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Languages: eng Pagination: 513-24 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, Texas 78229, USA. |
| Data Bank Information | |
Bank Name/Acc. No.:
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PDB/1YUW |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphate
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metabolism Amino Acid Substitution / genetics Animals Auxilins / metabolism Cattle Clathrin / metabolism Crystallization Crystallography, X-Ray Cysteine / genetics, metabolism Fluorometry HSP70 Heat-Shock Proteins / chemistry*, genetics, physiology* Humans Protein Structure, Tertiary / genetics Tryptophan / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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AQ-1486//PHS HHS; GM-52522/GM/NIGMS NIH HHS; NS29051/NS/NINDS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Auxilins; 0/Clathrin; 0/HSP70 Heat-Shock Proteins; 52-90-4/Cysteine; 56-65-5/Adenosine Triphosphate; 73-22-3/Tryptophan |
| Comments/Corrections | |
Comment In:
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Mol Cell. 2005 Nov 23;20(4):493-4
[PMID:
16307911
]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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