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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Archaeal Proteins*
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism
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Binding Sites
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Carrier Proteins / metabolism
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Chromatin / chemistry*
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Chromatin / metabolism
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Chromatography, High Pressure Liquid
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Chromobox Protein Homolog 5
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Chromosomal Proteins, Non-Histone / chemistry
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Chromosomal Proteins, Non-Histone / metabolism
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Cloning, Molecular
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / metabolism
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Magnetic Resonance Spectroscopy
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Mice
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Models, Molecular
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Molecular Sequence Data
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Solutions
Substances
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Archaeal Proteins
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Bacterial Proteins
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Carrier Proteins
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Chromatin
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Chromosomal Proteins, Non-Histone
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DNA-Binding Proteins
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Solutions
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Sso7d protein, Sulfolobus
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Chromobox Protein Homolog 5