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PMID: 12575990 Published · ppublish English Journal Article Review

Structure of SET domain proteins: a new twist on histone methylation.

Trends in biochemical sciences ·Vol. 28 ·No. 2 ·2003-02-00 ·Pages 59-62

Marmorstein R

Abstract

The methylation of lysine residues on histone tails is catalyzed by proteins containing a conserved SET domain. A recent flurry of structures of SET domain proteins has revealed a new protein fold and a scaffold for understanding catalysis and substrate binding by these enzymes. The prospect that histone methylation might form an epigenetic code and the implicated involvement of SET domain proteins in cancer assures that structure-function studies of these enzymes will continue until their detailed mechanism of action is determined.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Coenzymes/metabolism Conserved Sequence Histones/metabolism Humans Lysine/metabolism Methylation Methyltransferases/metabolism Models, Molecular Molecular Sequence Data Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment Substrate Specificity
Chemicals
Coenzymes Histones Methyltransferases Lysine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Marmorstein Ronen
The Wistar Institute, The Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA. marmor@wistar.upenn.edu
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
2003-02-00
Pages
59-62
Language
English
Region
England
NLM ID
7610674
Subset
IM
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