1DZ1
Mouse HP1 (M31) C terminal (shadow chromo) domain
Summary for 1DZ1
Entry DOI | 10.2210/pdb1dz1/pdb |
Related | 1AP0 |
Descriptor | MODIFIER 1 PROTEIN (1 entity in total) |
Functional Keywords | chromatin structure, chromo domain, heterochromatin protein protein interaction, dimeric |
Biological source | MUS MUSCULUS (HOUSE MOUSE) |
Cellular location | Nucleus : P83917 |
Total number of polymer chains | 2 |
Total formula weight | 16152.36 |
Authors | Brasher, S.V.,Smith, B.O.,Fogh, R.H.,Nietlispach, D.,Thiru, A.,Nielsen, P.R.,Broadhurst, R.W.,Ball, L.J.,Murzina, N.,Laue, E.D. (deposition date: 2000-02-11, release date: 2000-04-09, Last modification date: 2024-05-15) |
Primary citation | Brasher, S.V.,Smith, B.O.,Fogh, R.H.,Nietlispach, D.,Thiru, A.,Nielsen, P.R.,Broadhurst, R.W.,Ball, L.J.,Murzina, N.,Laue, E.D. The Structure of Mouse Hp1 Suggests a Unique Mode of Single Peptide Recognition by the Shadow Chromo Domain Dimer Embo J., 19:1587-, 2000 Cited by PubMed Abstract: The heterochromatin protein 1 (HP1) family of proteins is involved in gene silencing via the formation of heterochromatic structures. They are composed of two related domains: an N-terminal chromo domain and a C-terminal shadow chromo domain. Present results suggest that chromo domains may function as protein interaction motifs, bringing together different proteins in multi-protein complexes and locating them in heterochromatin. We have previously determined the structure of the chromo domain from the mouse HP1beta protein, MOD1. We show here that, in contrast to the chromo domain, the shadow chromo domain is a homodimer. The intact HP1beta protein is also dimeric, where the interaction is mediated by the shadow chromo domain, with the chromo domains moving independently of each other at the end of flexible linkers. Mapping studies, with fragments of the CAF1 and TIF1beta proteins, show that an intact, dimeric, shadow chromo domain structure is required for complex formation. PubMed: 10747027DOI: 10.1093/EMBOJ/19.7.1587 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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