Linked Life Data

7882155

Source:http://linkedlifedata.com/resource/pubmed/id/7882155

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1995-4-11
pubmed:abstractText
We have recently shown that the N-terminal ATPase fragment of hsp70 (1-375, composed of domains I and II) as well as the subsequent domain III (376-520) may share three-dimensional similarities with hsp60. In this study, we propose that domain III, common to the hsp60s and hsp70s is also found in the hsp90s and adopts a beta-alpha-beta Rossmann-folded structure which is encountered in the NAD-binding domain of dehydrogenases. Consequently, with the help of the domain IV (in hsp70s and hsp90s) or of hsp10/GroES (in hsp60s) and possibly that of auxilliary partners, the hsp molecules could act as "unfoldases" or "reset systems" by disrupting secondary structures through redox reactions on the main polypeptidic chain with which they interact. The models built on this hypothesis may open up a new way for understanding the chaperone functions within the folding/unfolding processes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0764-4469
pubmed:author
pubmed:issnType
Print
pubmed:volume
317
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
721-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Redox mechanism for the chaperone activity of heat shock proteins HSPs 60, 70 and 90 as suggested by hydrophobic cluster analysis: hypothesis.
pubmed:affiliation
Département des Macromolécules Biologiques, CNRS URA09, Universités Paris VI-Paris VII, France.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't