6D28

Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with the specific ligand NECA

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6D28 の概要

• エントリーDOI: 10.2210/pdb6d28/pdb
• 分子名称: Endoplasmin, N-ETHYL-5'-CARBOXAMIDO ADENOSINE, 1-METHOXY-2-(2-METHOXYETHOXY)ETHANE, ... (4 entities in total)
• 機能のキーワード: hsp90, grp94, neca, inhibitor, chaperone
• 由来する生物種: Canis lupus familiaris (Dog)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31498.26

構造登録者

Soldano, K.L.,Jivan, A.,Nicchitta, C.V.,Gewirth, D.T. (登録日: 2018-04-13, 公開日: 2018-05-16, 最終更新日: 2024-03-13)

主引用文献

Soldano, K.L.,Jivan, A.,Nicchitta, C.V.,Gewirth, D.T.
Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation.
J. Biol. Chem., 278:48330-48338, 2003

PubMed Abstract: GRP94, the endoplasmic reticulum (ER) paralog of the chaperone Hsp90, plays an essential role in the structural maturation or secretion of a subset of proteins destined for transport to the cell surface, such as the Toll-like receptors 2 and 4, and IgG, respectively. GRP94 differs from cytoplasmic Hsp90 by exhibiting very weak ATP binding and hydrolysis activity. GRP94 also binds selectively to a series of substituted adenosine analogs. The high resolution crystal structures at 1.75-2.1 A of the N-terminal and adjacent charged domains of GRP94 in complex with N-ethylcarboxamidoadenosine, radicicol, and 2-chlorodideoxyadenosine reveals a structural mechanism for ligand discrimination among hsp90 family members. The structures also identify a putative subdomain that may act as a ligand-responsive switch. The residues of the charged region fold into a disordered loop whose termini are ordered and continue the twisted beta sheet that forms the structural core of the N-domain. This continuation of the beta sheet past the charged domain suggests a structural basis for the association of the N-terminal and middle domains of the full-length chaperone.

PubMed: 12970348
DOI: 10.1074/jbc.M308661200

実験手法

X-RAY DIFFRACTION (1.75 Å)