1bgq
From Proteopedia
(New page: 200px<br /><applet load="1bgq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bgq, resolution 2.50Å" /> '''RADICICOL BOUND TO T...) |
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| - | [[Image:1bgq.gif|left|200px]]<br /><applet load="1bgq" size=" | + | [[Image:1bgq.gif|left|200px]]<br /><applet load="1bgq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bgq, resolution 2.50Å" /> | caption="1bgq, resolution 2.50Å" /> | ||
'''RADICICOL BOUND TO THE ATP BINDING SITE OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE'''<br /> | '''RADICICOL BOUND TO THE ATP BINDING SITE OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The cellular activity of several regulatory and signal transduction | + | The cellular activity of several regulatory and signal transduction proteins, which depend on the Hsp90 molecular chaperone for folding, is markedly decreased by geldanamycin and by radicicol (monorden). We now show that these unrelated compounds both bind to the N-terminal ATP/ADP-binding domain of Hsp90, with radicicol displaying nanomolar affinity, and both inhibit the inherent ATPase activity of Hsp90 which is essential for its function in vivo. Crystal structure determinations of Hsp90 N-terminal domain complexes with geldanamycin and radicicol identify key aspects of their nucleotide mimicry and suggest a rational basis for the design of novel antichaperone drugs. |
==About this Structure== | ==About this Structure== | ||
| - | 1BGQ 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 RDC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1BGQ 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 <scene name='pdbligand=RDC:'>RDC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Pearl, L | + | [[Category: Pearl, L H.]] |
[[Category: Prodromou, C.]] | [[Category: Prodromou, C.]] | ||
| - | [[Category: Roe, S | + | [[Category: Roe, S M.]] |
[[Category: RDC]] | [[Category: RDC]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
| Line 22: | Line 22: | ||
[[Category: inhibitor]] | [[Category: inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:04 2008'' |
Revision as of 09:55, 21 February 2008
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RADICICOL BOUND TO THE ATP BINDING SITE OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE
Overview
The cellular activity of several regulatory and signal transduction proteins, which depend on the Hsp90 molecular chaperone for folding, is markedly decreased by geldanamycin and by radicicol (monorden). We now show that these unrelated compounds both bind to the N-terminal ATP/ADP-binding domain of Hsp90, with radicicol displaying nanomolar affinity, and both inhibit the inherent ATPase activity of Hsp90 which is essential for its function in vivo. Crystal structure determinations of Hsp90 N-terminal domain complexes with geldanamycin and radicicol identify key aspects of their nucleotide mimicry and suggest a rational basis for the design of novel antichaperone drugs.
About this Structure
1BGQ is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin., Roe SM, Prodromou C, O'Brien R, Ladbury JE, Piper PW, Pearl LH, J Med Chem. 1999 Jan 28;42(2):260-6. PMID:9925731
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