2kyx: Difference between revisions

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-{{Seed}}
-[[Image:2kyx.jpg|left|200px]]
-<!--
+==Solution structure of the RRM domain of CYP33==
-The line below this paragraph, containing "STRUCTURE_2kyx", creates the "Structure Box" on the page.
+<StructureSection load='2kyx' size='340' side='right'caption='[[2kyx]]' 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'>[[2kyx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KYX 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">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=2kyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyx OCA], [https://pdbe.org/2kyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kyx RCSB], [https://www.ebi.ac.uk/pdbsum/2kyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kyx ProSAT]</span></td></tr>
-{{STRUCTURE_2kyx|  PDB=2kyx  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PPIE_HUMAN PPIE_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing.
+== 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/ky/2kyx_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=2kyx ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The mixed lineage leukemia (MLL) gene plays a critical role in epigenetic regulation of gene expression and is a frequent target of chromosomal translocations leading to leukemia. MLL plant homeodomain 3 (PHD3) is lost in all MLL translocation products, and reinsertion of PHD3 into MLL fusion proteins abrogates their transforming activity. PHD3 has been shown to interact with the RNA-recognition motif (RRM) domain of human nuclear Cyclophilin33 (CYP33). Here, we show that CYP33 mediates downregulation of the expression of MLL target genes HOXC8, HOXA9, CDKN1B, and C-MYC, in a proline isomerase-dependent manner. This downregulation correlates with the reduction of trimethylated lysine 4 of histone H3 (H3K4me3) and histone H3 acetylation. We have structurally characterized both the PHD3 and CYP33 RRM domains and analyzed their binding to one another. The PHD3 domain binds H3K4me3 (preferentially) and the CYP33 RRM domain at distinct sites. Our binding data show that binding of H3K4me3 to PHD3 and binding of the CYP33 RRM domain to PHD3 are mutually inhibitory, implying that PHD3 is a molecular switch for the transition between activation and repression of target genes. To explore the possible mechanism of CYP33/PHD3-mediated repression, we have analyzed the CYP33 proline isomerase activity on various H3 and H4 peptides and shown selectivity for two sites in H3. Our results provide a possible mechanism for the MLL PHD3 domain to act as a switch between activation and repression.
-===Solution structure of the RRM domain of CYP33===
+The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-mediated activation and repression .,Park S, Osmers U, Raman G, Schwantes RH, Diaz MO, Bushweller JH Biochemistry. 2010 Aug 10;49(31):6576-86. PMID:20677832<ref>PMID:20677832</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2kyx" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_20677832}}, adds the Publication Abstract to the page
+*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 20677832 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20677832}}
+__TOC__
+</StructureSection>
-==About this Structure==
-KYX is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYX OCA].
-==Reference==
-<ref group="xtra">PMID:20677832</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Large Structures]]
-[[Category: Bushweller, J H.]]
+[[Category: Bushweller JH]]
-[[Category: Park, S.]]
+[[Category: Park S]]
-[[Category: Cyp33]]
-[[Category: Isomerase]]
-[[Category: Rrm]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 25 08:46:30 2010''