The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A

被引：9
作者：
Tsai, Meng-Lin [1 ]
Cronin, Nora [2 ]
Djordjevic, Snezana [1 ]
机构：
[1] UCL, Div Biosci, Inst Struct & Mol Biol, London WC1E 6BT, England
[2] Univ London, Birkbeck Coll, Inst Struct & Mol Biol, London WC1E 7HX, England
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2011年 / 67卷
基金：
英国生物技术与生命科学研究理事会;
关键词：
signal transduction; protein phosphatase 2A; methyltransferases; methylation; protein phosphatase methylesterases; CATALYTIC SUBUNIT; ENDOTHELIAL-CELLS; CRYSTAL-STRUCTURE; 2A; KINASE; DEPHOSPHORYLATION; PHOSPHORYLATION; INACTIVATION; METHYLATION; ACTIVATION;
D O I：
10.1107/S0907444910042204
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 A. 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.
引用
收藏
页码：14 / 24
页数：11
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