1dz1

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(New page: 200px<br /><applet load="1dz1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dz1" /> '''MOUSE HP1 (M31) C TERMINAL (SHADOW CHROMO) D...)
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'''MOUSE HP1 (M31) C TERMINAL (SHADOW CHROMO) DOMAIN'''<br />
'''MOUSE HP1 (M31) C TERMINAL (SHADOW CHROMO) DOMAIN'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1DZ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZ1 OCA].
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1DZ1 is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Ball, L.J.]]
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[[Category: Ball, L J.]]
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[[Category: Brasher, S.V.]]
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[[Category: Brasher, S V.]]
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[[Category: Broadhurst, R.W.]]
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[[Category: Broadhurst, R W.]]
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[[Category: Fogh, R.H.]]
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[[Category: Fogh, R H.]]
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[[Category: Laue, E.D.]]
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[[Category: Laue, E D.]]
[[Category: Murzina, N.]]
[[Category: Murzina, N.]]
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[[Category: Nielsen, P.R.]]
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[[Category: Nielsen, P R.]]
[[Category: Nietlispach, D.]]
[[Category: Nietlispach, D.]]
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[[Category: Smith, B.O.]]
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[[Category: Smith, B O.]]
[[Category: Thiru, A.]]
[[Category: Thiru, A.]]
[[Category: chromatin structure]]
[[Category: chromatin structure]]
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[[Category: homodimer]]
[[Category: homodimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:41:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:01 2008''

Revision as of 10:22, 21 February 2008


1dz1

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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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