Solution structure of the SWIRM domain of human histone demethylase LSD1

Structure. 2006 Mar;14(3):457-68. doi: 10.1016/j.str.2005.12.004.

Abstract

SWIRM is an evolutionarily conserved domain involved in several chromatin-modifying complexes. Recently, the LSD1 protein, which bears a SWIRM domain, was found to be a demethylase for Lys4-methylated histone H3. Here, we report a solution structure of the SWIRM domain of human LSD1. It forms a compact fold composed of 6 alpha helices, in which a 20 amino acid long helix (alpha4) is surrounded by 5 other short helices. The SWIRM domain structure could be divided into the N-terminal part (alpha1-alpha3) and the C-terminal part (alpha4-alpha6), which are connected to each other by a salt bridge. While the N-terminal part forms a SWIRM-specific structure, the C-terminal part adopts a helix-turn-helix (HTH)-related fold. We discuss a model in which the SWIRM domain acts as an anchor site for a histone tail.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Chromatin Assembly and Disassembly*
  • DNA-Binding Proteins
  • Helix-Turn-Helix Motifs*
  • Histone Demethylases
  • Histones / analysis
  • Histones / metabolism
  • Models, Molecular*
  • Molecular Sequence Data
  • Oxidoreductases, N-Demethylating / chemistry
  • Oxidoreductases, N-Demethylating / genetics*
  • Protein Conformation
  • Protein Structure, Tertiary
  • Substrate Specificity
  • Time Factors
  • Transcription Factors / analysis
  • Transcription Factors / chemistry*

Substances

  • DNA-Binding Proteins
  • Histones
  • Transcription Factors
  • Histone Demethylases
  • KDM1A protein, human
  • Oxidoreductases, N-Demethylating

Associated data

  • PDB/2COM