1ah8: Difference between revisions

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{{Seed}}
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{{STRUCTURE_1ah8|  PDB=1ah8  |  SCENE=  }}  
{{STRUCTURE_1ah8|  PDB=1ah8  |  SCENE=  }}  


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




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_9187656}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_9187656}}


==About this Structure==
==About this Structure==
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[[Category: Chaperone]]
[[Category: Chaperone]]
[[Category: Heat shock]]
[[Category: Heat shock]]
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