Structures of SET domain proteins: protein lysine methyltransferases make their mark

Cell. 2002 Oct 4;111(1):5-7. doi: 10.1016/s0092-8674(02)01010-3.

Abstract

Proteins bearing the widely distributed SET domain have been shown to methylate lysine residues in histones and other proteins. In this issue, three-dimensional structures are reported for three very different SET domain-containing proteins. The structures reveal novel folds for several new domains, including SET, and provide early insights into mechanisms of catalysis and molecular recognition in this family of enzymes.

Publication types

  • Review

MeSH terms

  • Binding Sites
  • DNA-Binding Proteins / chemistry*
  • Drosophila Proteins / chemistry*
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase / chemistry*
  • Histones / chemistry
  • Methyltransferases / chemistry
  • Models, Molecular
  • Neurospora / metabolism
  • Nuclear Proteins / chemistry*
  • Polycomb Repressive Complex 2
  • Protein Conformation
  • Protein Methyltransferases
  • Protein Structure, Tertiary
  • Repressor Proteins / chemistry*
  • Ribulose-Bisphosphate Carboxylase / chemistry
  • Transcription Factors*

Substances

  • DNA-Binding Proteins
  • Drosophila Proteins
  • Histones
  • Nuclear Proteins
  • Repressor Proteins
  • Transcription Factors
  • Trl protein, Drosophila
  • Histone Methyltransferases
  • Methyltransferases
  • Protein Methyltransferases
  • E(z) protein, Drosophila
  • Histone-Lysine N-Methyltransferase
  • Polycomb Repressive Complex 2
  • Ribulose-Bisphosphate Carboxylase