1ah8

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(New page: 200px<br /><applet load="1ah8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ah8, resolution 2.10&Aring;" /> '''STRUCTURE OF THE ORT...)
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[[Image:1ah8.gif|left|200px]]<br /><applet load="1ah8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ah8, resolution 2.10&Aring;" />
caption="1ah8, resolution 2.10&Aring;" />
'''STRUCTURE OF THE ORTHORHOMBIC FORM OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE'''<br />
'''STRUCTURE OF THE ORTHORHOMBIC FORM OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE'''<br />
==Overview==
==Overview==
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Hsp90 is a highly specific chaperone for many signal transduction, proteins, including steroid hormone receptors and a broad range of protein, kinases. The crystal structure of the N-terminal domain of the yeast Hsp90, reveals a dimeric structure based on a highly twisted sixteen stranded, beta-sheet, whose topology suggests a possible 30-domain-swapped structure, for the intact Hsp90 dimer. The opposing faces of the beta-sheets in the, dimer define a potential peptide-binding cleft, suggesting that the, N-domain may serve as a molecular 'clamp' in the binding of ligand, proteins to Hsp90.
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Hsp90 is a highly specific chaperone for many signal transduction proteins, including steroid hormone receptors and a broad range of protein kinases. The crystal structure of the N-terminal domain of the yeast Hsp90 reveals a dimeric structure based on a highly twisted sixteen stranded beta-sheet, whose topology suggests a possible 30-domain-swapped structure for the intact Hsp90 dimer. The opposing faces of the beta-sheets in the dimer define a potential peptide-binding cleft, suggesting that the N-domain may serve as a molecular 'clamp' in the binding of ligand proteins to Hsp90.
==About this Structure==
==About this Structure==
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1AH8 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 GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AH8 OCA].
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1AH8 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=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AH8 OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Pearl, L.H.]]
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[[Category: Pearl, L H.]]
[[Category: Prodromou, C.]]
[[Category: Prodromou, C.]]
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[[Category: Roe, S.M.]]
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[[Category: Roe, S M.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: atp-binding]]
[[Category: atp-binding]]
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[[Category: heat shock]]
[[Category: heat shock]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:50:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:44:26 2008''

Revision as of 09:44, 21 February 2008


1ah8, resolution 2.10Å

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STRUCTURE OF THE ORTHORHOMBIC FORM OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE

Overview

Hsp90 is a highly specific chaperone for many signal transduction proteins, including steroid hormone receptors and a broad range of protein kinases. The crystal structure of the N-terminal domain of the yeast Hsp90 reveals a dimeric structure based on a highly twisted sixteen stranded beta-sheet, whose topology suggests a possible 30-domain-swapped structure for the intact Hsp90 dimer. The opposing faces of the beta-sheets in the dimer define a potential peptide-binding cleft, suggesting that the N-domain may serve as a molecular 'clamp' in the binding of ligand proteins to Hsp90.

About this Structure

1AH8 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

Reference

A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone., Prodromou C, Roe SM, Piper PW, Pearl LH, Nat Struct Biol. 1997 Jun;4(6):477-82. PMID:9187656

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