1am1
From Proteopedia
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| - | [[Image:1am1.jpg|left|200px]] | + | [[Image:1am1.jpg|left|200px]] |
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| - | '''ATP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE''' | + | {{Structure |
| + | |PDB= 1am1 |SIZE=350|CAPTION= <scene name='initialview01'>1am1</scene>, resolution 2.00Å | ||
| + | |SITE= <scene name='pdbsite=S1:Atp+Binding+Site'>S1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ATP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AM1 is a [ | + | 1AM1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AM1 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9230303 9230303] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nucleotide binding site]] | [[Category: nucleotide binding site]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:23 2008'' |
Revision as of 07:59, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
ATP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE
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 previously suggested. These results finally resolve the question of the direct involvement of ATP in Hsp90 function.
About this Structure
1AM1 is a Single protein structure of sequence from Saccharomyces cerevisiae. 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
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