Tsai, Meng-Lin and Cronin, Nora and Djordjevic, Snezana (2011) The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A. Acta Crystallographica Section D Biological Crystallography 67 (1), pp. 14-24. ISSN 0907-4449.
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.
Metadata
| Item Type: | Article |
|---|---|
| Keyword(s) / Subject(s): | signal transduction, protein phosphatase 2A, methyltransferases, methylation, protein phosphatase methylesterases |
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Depositing User: | Administrator |
| Date Deposited: | 14 Feb 2011 14:29 |
| Last Modified: | 02 Aug 2023 16:54 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/3052 |
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