Structural Chemistry of Human SET Domain Protein Methyltransferases
Matthieu Schapira*, 1, 2
Identifiers and Pagination:Year: 2011
Issue: Suppl 1
First Page: 85
Last Page: 94
Publisher Id: CCGTM-5-85
Article History:Received Date: 27/1/2011
Revision Received Date: 6/4/2011
Acceptance Date: 25/4/2011
Electronic publication date: 22/8/2011
Collection year: 2011
open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.
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.