Linked Life Data

16565516

Source:http://linkedlifedata.com/resource/pubmed/id/16565516

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2006-5-15
pubmed:abstractText
The co-chaperone p23 forms a complex with the chaperone Hsp90 that mediates the folding pathway leading to the production of functional steroid receptors. Solution NMR spectroscopy has been used to characterize sites of interaction between Hsp90 and p23. Titration of p23 with Hsp90 results in the selective broadening of certain cross-peaks in the 15N-1H heteronuclear single quantum correlation (HSQC) spectrum. The interaction sites on p23 and Hsp90 have been localized by dissection of Hsp90 into single-domain and two-domain constructs. The N-terminal (N) domain of Hsp90 does not affect the NMR spectrum of p23 either in the presence or absence of the ATP analogue ATPgammaS. Similarly, the HSQC spectrum of 15N-labeled N domain is unperturbed by the addition of p23. A subset of cross-peaks in the HSQC spectrum of p23 is shifted upon addition of the middle (M) domain of Hsp90, and the same shifts are observed upon the addition of the two-domain construct containing the N and M domains (NM). The addition of the co-chaperone Aha1, which is known to bind to the M domain of Hsp90, displaces p23 from Hsp90. The resonances that shift upon addition of the M and NM Hsp90 constructs correspond to those that were broadened at the lowest ratios of full-length Hsp90 to p23 and define an Hsp90 binding site that includes much of the C-terminal sequence of p23 together with a contiguous beta-hairpin from the N terminus. We conclude that p23 forms a specific complex with Hsp90 primarily through binding to its middle domain.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
281
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14457-64
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Localization of sites of interaction between p23 and Hsp90 in solution.
pubmed:affiliation
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural