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1DZ1

Mouse HP1 (M31) C terminal (shadow chromo) domain

Summary for 1DZ1
Entry DOI10.2210/pdb1dz1/pdb
Related1AP0
DescriptorMODIFIER 1 PROTEIN (1 entity in total)
Functional Keywordschromatin structure, chromo domain, heterochromatin protein protein interaction, dimeric
Biological sourceMUS MUSCULUS (HOUSE MOUSE)
Cellular locationNucleus : P83917
Total number of polymer chains2
Total formula weight16152.36
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 citationBrasher, 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: 10747027
DOI: 10.1093/EMBOJ/19.7.1587
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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