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1dz1

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

Structural highlights

1dz1 is a 2 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBX1_MOUSE Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Brasher SV, Smith BO, Fogh RH, Nietlispach D, Thiru A, Nielsen PR, Broadhurst RW, Ball LJ, Murzina NV, Laue ED. The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer. EMBO J. 2000 Apr 3;19(7):1587-97. PMID:10747027 doi:10.1093/emboj/19.7.1587

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dz1"

@@ Line 1: / Line 1: @@
 ==Mouse HP1 (M31) C terminal (shadow chromo) domain==
-<StructureSection load='1dz1' size='340' side='right' caption='[[1dz1]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>
+<StructureSection load='1dz1' size='340' side='right'caption='[[1dz1]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dz1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZ1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dz1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZ1 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ap0|1ap0]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dz1 OCA], [http://pdbe.org/1dz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dz1 RCSB], [http://www.ebi.ac.uk/pdbsum/1dz1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dz1 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dz1 OCA], [https://pdbe.org/1dz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dz1 RCSB], [https://www.ebi.ac.uk/pdbsum/1dz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dz1 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CBX1_MOUSE CBX1_MOUSE] Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Ball, L J]]
+[[Category: Mus musculus]]
-[[Category: Brasher, S V]]
+[[Category: Ball LJ]]
-[[Category: Broadhurst, R W]]
+[[Category: Brasher SV]]
-[[Category: Fogh, R H]]
+[[Category: Broadhurst RW]]
-[[Category: Laue, E D]]
+[[Category: Fogh RH]]
-[[Category: Murzina, N]]
+[[Category: Laue ED]]
-[[Category: Nielsen, P R]]
+[[Category: Murzina N]]
-[[Category: Nietlispach, D]]
+[[Category: Nielsen PR]]
-[[Category: Smith, B O]]
+[[Category: Nietlispach D]]
-[[Category: Thiru, A]]
+[[Category: Smith BO]]
-[[Category: Chromatin structure]]
+[[Category: Thiru A]]
-[[Category: Chromo domain]]
-[[Category: Dimeric]]
-[[Category: Heterochromatin protein protein interaction]]

1dz1

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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