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Structural Chemistry of Human SET Domain Protein Methyltransferases.

ABSTRACT: There are about fifty SET domain protein methyltransferases (PMTs) in the human genome, that transfer a methyl group from S-adenosyl-L-methionine (SAM) to substrate lysines on histone tails or other peptides. A number of structures in complex with cofactor, substrate, or inhibitors revealed the mechanisms of substrate recognition, methylation state specificity, and chemical inhibition. Based on these structures, we review the structural chemistry of SET domain PMTs, and propose general concepts towards the development of selective inhibitors.

SUBMITTER: Schapira M

PROVIDER: S-EPMC3178901 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

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Structural Chemistry of Human SET Domain Protein Methyltransferases.

Schapira Matthieu M

Current chemical genomics 20110822 Suppl 1

There are about fifty SET domain protein methyltransferases (PMTs) in the human genome, that transfer a methyl group from S-adenosyl-L-methionine (SAM) to substrate lysines on histone tails or other peptides. A number of structures in complex with cofactor, substrate, or inhibitors revealed the mechanisms of substrate recognition, methylation state specificity, and chemical inhibition. Based on these structures, we review the structural chemistry of SET domain PMTs, and propose general concepts ...[more]

PMID: 21966348

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