2XGO

XcOGT in complex with UDP-S-GlcNAc

2XGO の概要

• エントリーDOI: 10.2210/pdb2xgo/pdb
• 関連するPDBエントリー: 2JLB 2VSY 2XGM 2XGS
• 分子名称: XCOGT, URIDINE-DIPHOSPHATE-1-DEOXY-1-THIO-N-ACETYLGLUCOSAMINE (3 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: XANTHOMONAS CAMPESTRIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 123472.79

構造登録者

Dorfmueller, H.C.,Borodkin, V.S.,Blair, D.E.,Pathak, S.,Navratilova, I.,van Aalten, D.M. (登録日: 2010-06-07, 公開日: 2010-08-25, 最終更新日: 2023-12-20)

主引用文献

Dorfmueller, H.C.,Borodkin, V.S.,Blair, D.E.,Pathak, S.,Navratilova, I.,Van Aalten, D.M.
Substrate and Product Analogues as Human O-Glcnac Transferase Inhibitors.
Amino Acids, 40:781-, 2011

PubMed Abstract: Protein glycosylation on serine/threonine residues with N-acetylglucosamine (O-GlcNAc) is a dynamic, inducible and abundant post-translational modification. It is thought to regulate many cellular processes and there are examples of interplay between O-GlcNAc and protein phosphorylation. In metazoa, a single, highly conserved and essential gene encodes the O-GlcNAc transferase (OGT) that transfers GlcNAc onto substrate proteins using UDP-GlcNAc as the sugar donor. Specific inhibitors of human OGT would be useful tools to probe the role of this post-translational modification in regulating processes in the living cell. Here, we describe the synthesis of novel UDP-GlcNAc/UDP analogues and evaluate their inhibitory properties and structural binding modes in vitro alongside alloxan, a previously reported weak OGT inhibitor. While the novel analogues are not active on living cells, they inhibit the enzyme in the micromolar range and together with the structural data provide useful templates for further optimisation.

PubMed: 20640461
DOI: 10.1007/S00726-010-0688-Y

実験手法

X-RAY DIFFRACTION (2.6 Å)