1ah8 | pdb_00001ah8
STRUCTURE OF THE ORTHORHOMBIC FORM OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE
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| 1ah8, resolution 2.10Å | |||||||||||||
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| Ligands: | GOL | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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