The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A.
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Tsai ML, Cronin N, Djordjevic S
The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A.
Acta Crystallogr D Biol Crystallogr. 2011 Jan;67(Pt 1):14-24. doi: 10.1107/S0907444910042204. Epub 2010 Dec 16.
- PubMed ID
- 21206058 [ View in 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 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.