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2jv0

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[[Image:2jv0.png|left|200px]]
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==SET domain of RIZ1 tumor suppressor (PRDM2)==
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<StructureSection load='2jv0' size='340' side='right' caption='[[2jv0]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>
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== Structural highlights ==
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[[2jv0]] 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=2JV0 OCA]. <br>
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<b>Related:</b> [[2qpw|2qpw]]<br>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jv/2jv0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
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RIZ1 is a transcriptional regulator and tumor suppressor that catalyzes methylation of lysine 9 of histone H3. It contains a distinct SET domain, sometimes referred to as PR (PRDI-BF1 and RIZ1 homology) domain, that is responsible for its catalytic activity. We determined the solution structure of the PR domain from RIZ1 and characterized its interaction with S-adenosyl-l-homocysteine (SAH) and a peptide from histone H3. Despite low sequence identity with canonical SET domains, the PR domain displays a typical SET fold including a pseudo-knot at the C-terminus. The N-flanking sequence of RIZ1 PR domain adopts a novel conformation and interacts closely with the SET fold. The C-flanking sequence contains an alpha-helix that points away from the protein face that harbors active site in other SET domains. The SET fold of RIZ1 does not have detectable affinity for SAH but it interacts with a synthetic peptide comprising residues 1-20 of histone H3.
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Structural studies of the SET domain from RIZ1 tumor suppressor.,Briknarova K, Zhou X, Satterthwait A, Hoyt DW, Ely KR, Huang S Biochem Biophys Res Commun. 2008 Feb 15;366(3):807-13. Epub 2007 Dec 17. PMID:18082620<ref>PMID:18082620</ref>
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The line below this paragraph, containing "STRUCTURE_2jv0", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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-->
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{{STRUCTURE_2jv0| PDB=2jv0 | SCENE= }}
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===SET domain of RIZ1 tumor suppressor (PRDM2)===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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<!--
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__TOC__
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The line below this paragraph, {{ABSTRACT_PUBMED_18082620}}, adds the Publication Abstract to the page
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</StructureSection>
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(as it appears on PubMed at http://www.pubmed.gov), where 18082620 is the PubMed ID number.
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-->
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{{ABSTRACT_PUBMED_18082620}}
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==About this Structure==
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[[2jv0]] 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=2JV0 OCA].
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==Reference==
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<ref group="xtra">PMID:018082620</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Briknarova, K.]]
[[Category: Briknarova, K.]]

Revision as of 08:26, 30 April 2014

SET domain of RIZ1 tumor suppressor (PRDM2)

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