6EOU

O-GlcNAc transferase TPR domain with the intellectual disability associated mutation L254F

6EOU の概要

• エントリーDOI: 10.2210/pdb6eou/pdb
• 分子名称: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (2 entities in total)
• 機能のキーワード: intellectual disability associated point mutation in o-glcnac transferase tetratricopeptide domain, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43540.25

構造登録者

Gundogdu, M.,van Aalten, D.M.F. (登録日: 2017-10-10, 公開日: 2018-05-09, 最終更新日: 2024-01-17)

主引用文献

Gundogdu, M.,Llabres, S.,Gorelik, A.,Ferenbach, A.T.,Zachariae, U.,van Aalten, D.M.F.
The O-GlcNAc Transferase Intellectual Disability Mutation L254F Distorts the TPR Helix.
Cell Chem Biol, 25:513-518.e4, 2018

PubMed Abstract: O-linked β-N-acetyl--glucosamine (O-GlcNAc) transferase (OGT) regulates protein O-GlcNAcylation, an essential post-translational modification that is abundant in the brain. Recently, OGT mutations have been associated with intellectual disability, although it is not understood how they affect OGT structure and function. Using a multi-disciplinary approach we show that the L254F OGT mutation leads to conformational changes of the tetratricopeptide repeats and reduced activity, revealing the molecular mechanisms contributing to pathogenesis.

PubMed: 29606577
DOI: 10.1016/j.chembiol.2018.03.004

実験手法

X-RAY DIFFRACTION (1.75 Å)