Linked Life Data

7906860

Source:http://linkedlifedata.com/resource/pubmed/id/7906860

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1994-3-28
pubmed:abstractText
A cell-free system was used to examine heat shock protein 90 (hsp90)-progesterone receptor (PR) binding at near physiological conditions. Four major findings are presented: 1) hsp90 is required to maintain ligand binding by PR at elevated temperatures; 2) hsp70 and heat shock-related protein p60 are components of an intermediate assembly complex that precedes formation of a mature hsp90-PR complex; 3) hsp90-PR complexes are in a steady state assembly/disassembly cycle (t1/2, 5 min); and 4) hsp90 dissociation is not accelerated after progesterone binding; instead, progesterone prevents PR from forming hsp70-mediated assembly complexes. A model incorporating these findings is presented in which unliganded PR is maintained in a disactivation loop of assembly/disassembly with hsp90; hormone binding releases PR from this loop to proceed along an activation pathway.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0888-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1418-29
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes.
pubmed:affiliation
Department of Pharmacology, University of Nebraska Medical Center, Omaha 68198.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.