1a4h
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1a4h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a4h, resolution 2.50Å" /> '''STRUCTURE OF THE N-...)
Next diff →
Revision as of 16:14, 29 October 2007
|
STRUCTURE OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE IN COMPLEX WITH GELDANAMYCIN
Overview
Hsp90 molecular chaperones in eukaryotic cells play essential roles in the, folding and activation of a range of client proteins involved in cell, cycle regulation, steroid hormone responsiveness, and signal transduction., The biochemical mechanism of Hsp90 is poorly understood, and the, involvement of ATP in particular is controversial. Crystal structures of, complexes between the N-terminal domain of the yeast Hsp90 chaperone and, ADP/ATP unambiguously identify a specific adenine nucleotide binding site, homologous to the ATP-binding site of DNA gyrase B. This site is the same, as that identified for the antitumor agent geldanamycin, suggesting that, geldanamycin acts by blocking the binding of nucleotides to Hsp90 and not, the binding of incompletely folded client polypeptides as ... [(full description)]
About this Structure
1A4H is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with GMY as [ligand]. Full crystallographic information is available from [OCA].
Reference
Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone., Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH, Cell. 1997 Jul 11;90(1):65-75. PMID:9230303
Page seeded by OCA on Mon Oct 29 18:19:08 2007
