Linked Life Data

9826495

Source:http://linkedlifedata.com/resource/pubmed/id/9826495

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-1-25
pubmed:abstractText
Dimerization of the DNA-binding domains of nuclear hormone receptors occurs in a manner that is highly cooperative with DNA binding. We have investigated the molecular basis for this cooperativity through an NMR study of the interaction between the monomeric DNA-binding domain (DBD) of the retinoid-X-receptor (RXR) and a single DNA half-site. Major changes were observed in the chemical shifts of the backbone resonances and in the pattern of medium-range nuclear Overhauser enhancement connectivities of the RXR upon binding to DNA, indicating that the DNA induces conformational changes in the monomer. Binding to DNA induces and stabilizes the structure in a region of the second zinc binding domain that forms the dimerization interface when RXR binds as a dimer to a direct repeat recognition element. These studies provide direct experimental evidence that DNA-induced protein conformational changes constitute the molecular basis for cooperative enhancement of dimer formation and DNA binding by the nuclear hormone receptor DBDs. In contrast to the localized folding induced in the dimerization interface, DNA binding leads to unfolding of the C-terminal helix found in the free RXR DBD. Unwinding of this helix may facilitate homodimer formation by maximizing interactions between the two DNA-bound RXR domains.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 1998 Academic Press
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
284
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
533-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
DNA-induced conformational changes are the basis for cooperative dimerization by the DNA binding domain of the retinoid X receptor.
pubmed:affiliation
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA, 92037, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't