3O7W

The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1

「3MNT」から置き換えられました

3O7W の概要

• エントリーDOI: 10.2210/pdb3o7w/pdb
• 分子名称: Leucine carboxyl methyltransferase 1, GLYCEROL, S-ADENOSYLMETHIONINE, ... (5 entities in total)
• 機能のキーワード: modified rossmann fold, transferase, pp2a
• 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: 34424.46

構造登録者

Tsai, M.L.,Cronin, N.,Djordjevic, S. (登録日: 2010-08-01, 公開日: 2010-09-08, 最終更新日: 2024-03-20)

主引用文献

Tsai, M.L.,Cronin, N.,Djordjevic, S.
The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A
Acta Crystallogr.,Sect.D, 67:14-24, 2011

PubMed Abstract: Leucine carboxyl methyltransferase 1 (LCMT1) methylates the terminal carboxyl group of the leucine 309 residue of human protein phosphatase 2A (PP2A). PP2A, a key regulator of many cellular processes, has recently generated additional interest as a potential cancer-therapeutic target. The status of PP2A methylation impacts upon the selection of the regulatory subunit by the PP2A core enzyme, thus directing its activity and subcellular localization. An X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet) has been solved to a resolution of 2 Å. The structure enables the postulation of a mode of interaction with protein phosphatase PP2A and provides a platform for further functional studies of the regulation of methylation of PP2A.

PubMed: 21206058
DOI: 10.1107/S0907444910042204

実験手法

X-RAY DIFFRACTION (2 Å)