Structure of the chromatin binding (chromo) domain from mouse modifier protein 1

L J Ball, N V Murzina, R W Broadhurst, A R Raine, S J Archer, F J Stott, A G Murzin, P B Singh, P J Domaille, E D Laue

Research output: Contribution to journalArticlepeer-review

146 Citations (Scopus)


The structure of a chromatin binding domain from mouse chromatin modifier protein 1 (MoMOD1) was determined using nuclear magnetic resonance (NMR) spectroscopy. The protein consists of an N-terminal three-stranded anti-parallel beta-sheet which folds against a C-terminal alpha-helix. The structure reveals an unexpected homology to two archaebacterial DNA binding proteins which are also involved in chromatin structure. Structural comparisons suggest that chromo domains, of which more than 40 are now known, act as protein interaction motifs and that the MoMOD1 protein acts as an adaptor mediating interactions between different proteins.

Original languageEnglish
Pages (from-to)2473-81
Number of pages9
JournalEMBO Journal
Issue number9
Publication statusPublished - May 1 1997


  • Amino Acid Sequence
  • Animals
  • Archaeal Proteins
  • Bacterial Proteins
  • Binding Sites
  • Carrier Proteins
  • Chromatin
  • Chromatography, High Pressure Liquid
  • Chromosomal Proteins, Non-Histone
  • Cloning, Molecular
  • DNA-Binding Proteins
  • Magnetic Resonance Spectroscopy
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Solutions
  • Journal Article
  • Research Support, Non-U.S. Gov't

Fingerprint Dive into the research topics of 'Structure of the chromatin binding (chromo) domain from mouse modifier protein 1'. Together they form a unique fingerprint.

Cite this