1uz3: Difference between revisions

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-{{Seed}}
-[[Image:1uz3.png|left|200px]]
-<!--
+==Crystal structure of novel protein EMSY==
-The line below this paragraph, containing "STRUCTURE_1uz3", creates the "Structure Box" on the page.
+<StructureSection load='1uz3' size='340' side='right'caption='[[1uz3]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1uz3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UZ3 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1&#8491;</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=1uz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uz3 OCA], [https://pdbe.org/1uz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uz3 RCSB], [https://www.ebi.ac.uk/pdbsum/1uz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uz3 ProSAT]</span></td></tr>
-{{STRUCTURE_1uz3|  PDB=1uz3  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/EMSY_HUMAN EMSY_HUMAN] Regulator which is able to repress transcription, possibly via its interaction with a multiprotein chromatin remodeling complex that modifies the chromatin. Its interaction with BRCA2 suggests that it may play a central role in the DNA repair function of BRCA2.<ref>PMID:14651845</ref>
+== 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/uz/1uz3_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=1uz3 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+EMSY is a recently discovered gene encoding a BRCA2-associated protein and is amplified in some sporadic breast and ovarian cancers. The EMSY sequence contains no known domain except for a conserved approximately 100 residue segment at the N terminus. This so-called ENT domain is unique in the human genome, although multiple copies are found in Arabidopsis proteins containing members of the Royal family of chromatin remodelling domains. Here, we report the crystal structure of the ENT domain of EMSY, consisting of a unique arrangement of five alpha-helices that fold into a helical bundle arrangement. The fold shares regions of structural homology with the DNA-binding domain of homeodomain proteins. The ENT domain forms a homodimer via the anti-parallel packing of the extended N-terminal alpha-helix of each molecule. It is stabilized mainly by hydrophobic residues at the dimer interface and has a dissociation constant in the low micromolar range. The dimerisation of EMSY mediated by the ENT domain could provide flexibility for it to bind two or more different substrates simultaneously.
-===CRYSTAL STRUCTURE OF NOVEL PROTEIN EMSY===
+Crystal structure of the ENT domain of human EMSY.,Chavali GB, Ekblad CM, Basu BP, Brissett NC, Veprintsev D, Hughes-Davies L, Kouzarides T, Itzhaki LS, Doherty AJ J Mol Biol. 2005 Jul 29;350(5):964-73. PMID:15978617<ref>PMID:15978617</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_15978617}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1uz3" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15978617 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15978617}}
+__TOC__
+</StructureSection>
-==About this Structure==
-UZ3 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UZ3 OCA].
-==Reference==
-<ref group="xtra">PMID:15978617</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Basu, B P.]]
+[[Category: Large Structures]]
-[[Category: Chavali, G B.]]
+[[Category: Basu BP]]
-[[Category: Doherty, A J.]]
+[[Category: Chavali GB]]
-[[Category: Chromatin regulator]]
+[[Category: Doherty AJ]]
-[[Category: Royal family domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:56:07 2009''