1dz1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1dz1" [edit=sysop:move=sysop])
Current revision (05:29, 15 May 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1dz1.png|left|200px]]
 
-
{{STRUCTURE_1dz1| PDB=1dz1 | SCENE= }}
+
==Mouse HP1 (M31) C terminal (shadow chromo) domain==
 +
<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 [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='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'>[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]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dz/1dz1_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dz1 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
===MOUSE HP1 (M31) C TERMINAL (SHADOW CHROMO) DOMAIN===
+
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<ref>PMID:10747027</ref>
-
{{ABSTRACT_PUBMED_10747027}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 1dz1" style="background-color:#fffaf0;"></div>
-
[[1dz1]] is a 2 chain structure with sequence from [http://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].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:010747027</ref><references group="xtra"/>
+
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Ball, L J.]]
+
[[Category: Ball LJ]]
-
[[Category: Brasher, S V.]]
+
[[Category: Brasher SV]]
-
[[Category: Broadhurst, R W.]]
+
[[Category: Broadhurst RW]]
-
[[Category: Fogh, R H.]]
+
[[Category: Fogh RH]]
-
[[Category: Laue, E D.]]
+
[[Category: Laue ED]]
-
[[Category: Murzina, N.]]
+
[[Category: Murzina N]]
-
[[Category: Nielsen, P R.]]
+
[[Category: Nielsen PR]]
-
[[Category: Nietlispach, D.]]
+
[[Category: Nietlispach D]]
-
[[Category: Smith, B O.]]
+
[[Category: Smith BO]]
-
[[Category: Thiru, A.]]
+
[[Category: Thiru A]]
-
[[Category: Chromatin structure]]
+
-
[[Category: Chromo domain]]
+
-
[[Category: Dimeric]]
+
-
[[Category: Heterochromatin protein protein interaction]]
+

Current revision

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

PDB ID 1dz1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools