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1ah8
From Proteopedia
(New page: 200px<br /><applet load="1ah8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ah8, resolution 2.10Å" /> '''STRUCTURE OF THE ORT...) |
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| - | [[Image:1ah8.gif|left|200px]]<br /><applet load="1ah8" size=" | + | [[Image:1ah8.gif|left|200px]]<br /><applet load="1ah8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ah8, resolution 2.10Å" /> | caption="1ah8, resolution 2.10Å" /> | ||
'''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== | ||
| - | Hsp90 is a highly specific chaperone for many signal transduction | + | 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== | ||
| - | 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:// | + | 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== | ||
| Line 13: | Line 13: | ||
[[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: GOL]] | [[Category: GOL]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
| Line 21: | Line 21: | ||
[[Category: heat shock]] | [[Category: heat shock]] | ||
| - | ''Page seeded by [http:// | + | ''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
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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
Page seeded by OCA on Thu Feb 21 11:44:26 2008
