4CE2

Hsp90 N-terminal domain bound to macrolactam analogues of radicicol.

4CE2 の概要

• エントリーDOI: 10.2210/pdb4ce2/pdb
• 関連するPDBエントリー: 4CE1 4CE3
• 分子名称: ATP-DEPENDENT MOLECULAR CHAPERONE HSP82, (9E)-19-CHLORANYL-13-METHYL-16,18-BIS(OXIDANYL)-13-AZABICYCLO[13.4.0]NONADECA-1(15),9,16,18-TETRAENE-3,14-DIONE (3 entities in total)
• 機能のキーワード: chaperone
• 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: 1
• 化学式量合計: 24574.43

構造登録者

Roe, S.M.,Parry-Morris, S.,Prodromou, C. (登録日: 2013-11-08, 公開日: 2014-01-29, 最終更新日: 2023-12-20)

主引用文献

Dutton, B.L.,Kitson, R.R.,Parry-Morris, S.,Roe, S.M.,Prodromou, C.,Moody, C.J.
Synthesis of macrolactam analogues of radicicol and their binding to heat shock protein Hsp90.
Org. Biomol. Chem., 12:1328-1340, 2014

PubMed Abstract: A series of macrolactam analogues of the naturally occurring resorcylic acid lactone radicicol have been synthesised from methyl orsellinate in 7 steps, involving chlorination, protection of the two phenolic groups, and hydrolysis to the benzoic acid. Formation of the dianion and quenching with a Weinreb amide results in acylation of the toluene methyl group that is followed by amide formation and ring closing metathesis to form the macrocyclic lactam. Final deprotection of the phenolic groups gives the desired macrolactams whose binding to the N-terminal domain of yeast Hsp90 was studied by isothermal titration calorimetry and protein X-ray crystallography.

PubMed: 24435512
DOI: 10.1039/c3ob42211a

実験手法

X-RAY DIFFRACTION (2.38 Å)