1AH8

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

1AH8 の概要

• エントリーDOI: 10.2210/pdb1ah8/pdb
• 分子名称: HEAT SHOCK PROTEIN 90, GLYCEROL (3 entities in total)
• 機能のキーワード: chaperone, atp-binding, heat shock
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P02829
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50115.17

構造登録者

Prodromou, C.,Roe, S.M.,Pearl, L.H. (登録日: 1997-04-14, 公開日: 1997-10-22, 最終更新日: 2024-04-03)

主引用文献

Prodromou, C.,Roe, S.M.,Piper, P.W.,Pearl, L.H.
A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone.
Nat.Struct.Biol., 4:477-482, 1997

PubMed Abstract: 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.

PubMed: 9187656
DOI: 10.1038/nsb0697-477

実験手法

X-RAY DIFFRACTION (2.1 Å)