5M7S

Structure of human O-GlcNAc hydrolase with bound transition state analog ThiametG

5M7S の概要

• エントリーDOI: 10.2210/pdb5m7s/pdb
• 分子名称: Protein O-GlcNAcase, (3AR,5R,6S,7R,7AR)-2-(ETHYLAMINO)-5-(HYDROXYMETHYL)-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D][1,3]THIAZOLE-6,7-DIOL (3 entities in total)
• 機能のキーワード: hoga o-glcnac, hydrolase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Isoform 3: Nucleus . Isoform 1: Cytoplasm : O60502
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 206538.41

構造登録者

Roth, C.,Chan, S.,Offen, W.A.,Hemsworth, G.R.,Willems, L.I.,King, D.,Varghese, V.,Britton, R.,Vocadlo, D.J.,Davies, G.J. (登録日: 2016-10-28, 公開日: 2017-03-29, 最終更新日: 2024-11-06)

主引用文献

Roth, C.,Chan, S.,Offen, W.A.,Hemsworth, G.R.,Willems, L.I.,King, D.T.,Varghese, V.,Britton, R.,Vocadlo, D.J.,Davies, G.J.
Structural and functional insight into human O-GlcNAcase.
Nat. Chem. Biol., 13:610-612, 2017

PubMed Abstract: O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual helix-exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors that have clinical value.

PubMed: 28346405
DOI: 10.1038/nchembio.2358

実験手法

X-RAY DIFFRACTION (2.4 Å)