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

TitleStructure of the chromatin binding (chromo) domain from mouse modifier protein 1.
Publication TypeJournal Article
Year of Publication1997
AuthorsBall, LJ, Murzina, NV, Broadhurst, RW, Raine, AR, Archer, SJ, Stott, FJ, Murzin, AG, Singh, PB, Domaille, PJ, Laue, ED
JournalEMBO J
Volume16
Issue9
Pagination2473-81
Date Published1997 May 01
ISSN0261-4189
KeywordsAmino 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
Abstract

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.

DOI10.1093/emboj/16.9.2473
Alternate JournalEMBO J.
Citation Key10.1093/emboj/16.9.2473
PubMed ID9171360
PubMed Central IDPMC1169847
Grant List / / Wellcome Trust / United Kingdom