1am1: Difference between revisions
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==Overview== | ==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 .. | 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 previously, suggested. These results finally resolve the question of the direct, involvement of ATP in Hsp90 function. | ||
==About this Structure== | ==About this Structure== | ||
1AM1 is a | 1AM1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: S1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AM1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: nucleotide binding site]] | [[Category: nucleotide binding site]] | ||
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Revision as of 14:29, 5 November 2007
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ATP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE
OverviewOverview
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 previously, suggested. These results finally resolve the question of the direct, involvement of ATP in Hsp90 function.
About this StructureAbout this Structure
1AM1 is a Single protein structure of sequence from Saccharomyces cerevisiae with ADP as ligand. Structure known Active Site: S1. Full crystallographic information is available from OCA.
ReferenceReference
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
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