Document Detail


An essential connection: link between Hsp70's domains at last.
MedLine Citation:
PMID:  16307911     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Communication between the ATPase and substrate binding domains of Hsp70 is critical for regulated interaction between this molecular chaperone and its client proteins. In this issue of Molecular Cell, Jiang et al. (2005) report the structure of an intact Hsp70, revealing critical interactions between the two domains.
Authors:
Patrick D'Silva; Jaroslaw Marszalek; Elizabeth A Craig
Publication Detail:
Type:  Comment; Journal Article    
Journal Detail:
Title:  Molecular cell     Volume:  20     ISSN:  1097-2765     ISO Abbreviation:  Mol. Cell     Publication Date:  2005 Nov 
Date Detail:
Created Date:  2005-11-25     Completed Date:  2006-01-05     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9802571     Medline TA:  Mol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  493-4     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, 433 Babcock Drive, University of Wisconsin, Madison, Madison, Wisconsin 53726, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
HSP70 Heat-Shock Proteins / chemistry*,  physiology*
Humans
Protein Structure, Tertiary
Chemical
Reg. No./Substance:
0/HSP70 Heat-Shock Proteins
Comments/Corrections
Comment On:
Mol Cell. 2005 Nov 23;20(4):513-24   [PMID:  16307916 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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