1dz1
From Proteopedia
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| - | [[Image:1dz1.gif|left|200px]] | + | [[Image:1dz1.gif|left|200px]] |
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| - | '''MOUSE HP1 (M31) C TERMINAL (SHADOW CHROMO) DOMAIN''' | + | {{Structure |
| + | |PDB= 1dz1 |SIZE=350|CAPTION= <scene name='initialview01'>1dz1</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''MOUSE HP1 (M31) C TERMINAL (SHADOW CHROMO) DOMAIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DZ1 is a [ | + | 1DZ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZ1 OCA]. |
==Reference== | ==Reference== | ||
| - | The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer., Brasher SV, Smith BO, Fogh RH, Nietlispach D, Thiru A, Nielsen PR, Broadhurst RW, Ball LJ, Murzina NV, Laue ED, EMBO J. 2000 Apr 3;19(7):1587-97. PMID:[http:// | + | The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer., Brasher SV, Smith BO, Fogh RH, Nietlispach D, Thiru A, Nielsen PR, Broadhurst RW, Ball LJ, Murzina NV, Laue ED, EMBO J. 2000 Apr 3;19(7):1587-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10747027 10747027] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: homodimer]] | [[Category: homodimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:46:46 2008'' |
Revision as of 08:46, 20 March 2008
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MOUSE HP1 (M31) C TERMINAL (SHADOW CHROMO) DOMAIN
Overview
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.
About this Structure
1DZ1 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer., Brasher SV, Smith BO, Fogh RH, Nietlispach D, Thiru A, Nielsen PR, Broadhurst RW, Ball LJ, Murzina NV, Laue ED, EMBO J. 2000 Apr 3;19(7):1587-97. PMID:10747027
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