2a7o: Difference between revisions

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New page: left|200px<br /> <applet load="2a7o" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a7o" /> '''Solution Structure of the hSet2/HYPB SRI do...
 
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[[Image:2a7o.gif|left|200px]]<br />
<applet load="2a7o" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2a7o" />
'''Solution Structure of the hSet2/HYPB SRI domain'''<br />


==Overview==
==Solution Structure of the hSet2/HYPB SRI domain==
The phosphorylation state of the C-terminal repeat domain (CTD) of the, largest subunit of RNA polymerase II changes as polymerase transcribes a, gene, and the distinct forms of the phospho-CTD (PCTD) recruit different, nuclear factors to elongating polymerase. The Set2 histone, methyltransferase from yeast was recently shown to bind the PCTD of, elongating RNA polymerase II by means of a novel domain termed the, Set2-Rpb1 interacting (SRI) domain. Here, we report the solution structure, of the SRI domain in human Set2 (hSRI domain), which adopts a left-turned, three-helix bundle distinctly different from other structurally, characterized PCTD-interacting domains. NMR titration experiments mapped, the binding surface of the hSRI domain to helices 1 and 2, and Biacore, binding studies showed that the domain binds preferably to [Ser-2 +, Ser-5]-phosphorylated CTD peptides containing two or more heptad repeats., Point-mutagenesis studies identified five residues critical for PCTD, binding. In view of the differential effects of these point mutations on, binding to different CTD phosphopeptides, we propose a model for the hSRI, domain interaction with the PCTD.
<StructureSection load='2a7o' size='340' side='right'caption='[[2a7o]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2a7o]] 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=2A7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7O 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=2a7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7o OCA], [https://pdbe.org/2a7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7o RCSB], [https://www.ebi.ac.uk/pdbsum/2a7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SETD2_HUMAN SETD2_HUMAN] Histone methyltransferase that methylates 'Lys-36' of histone H3. H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation. Probably plays a role in chromatin structure modulation during elongation via its interaction with hyperphosphorylated POLR2A. Binds DNA at promoters. May also act as a transcription activator that binds to promoters. Binds to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression.<ref>PMID:16118227</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/a7/2a7o_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=2a7o ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The phosphorylation state of the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II changes as polymerase transcribes a gene, and the distinct forms of the phospho-CTD (PCTD) recruit different nuclear factors to elongating polymerase. The Set2 histone methyltransferase from yeast was recently shown to bind the PCTD of elongating RNA polymerase II by means of a novel domain termed the Set2-Rpb1 interacting (SRI) domain. Here, we report the solution structure of the SRI domain in human Set2 (hSRI domain), which adopts a left-turned three-helix bundle distinctly different from other structurally characterized PCTD-interacting domains. NMR titration experiments mapped the binding surface of the hSRI domain to helices 1 and 2, and Biacore binding studies showed that the domain binds preferably to [Ser-2 + Ser-5]-phosphorylated CTD peptides containing two or more heptad repeats. Point-mutagenesis studies identified five residues critical for PCTD binding. In view of the differential effects of these point mutations on binding to different CTD phosphopeptides, we propose a model for the hSRI domain interaction with the PCTD.


==About this Structure==
Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1.,Li M, Phatnani HP, Guan Z, Sage H, Greenleaf AL, Zhou P Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17636-41. Epub 2005 Nov 28. PMID:16314571<ref>PMID:16314571</ref>
2A7O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A7O OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1., Li M, Phatnani HP, Guan Z, Sage H, Greenleaf AL, Zhou P, Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17636-41. Epub 2005 Nov 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16314571 16314571]
</div>
<div class="pdbe-citations 2a7o" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Greenleaf, A.]]
[[Category: Greenleaf A]]
[[Category: Guan, Z.]]
[[Category: Guan Z]]
[[Category: Li, M.]]
[[Category: Li M]]
[[Category: Phatnani, H.P.]]
[[Category: Phatnani HP]]
[[Category: Sage, H.]]
[[Category: Sage H]]
[[Category: Zhou, P.]]
[[Category: Zhou P]]
[[Category: hset2]]
[[Category: hsri]]
[[Category: pcap]]
[[Category: pcid]]
[[Category: phosphoctd associating protein]]
[[Category: set2]]
[[Category: set2 rpb1-interacting domain]]
[[Category: sri]]
[[Category: sri domain]]
 
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Latest revision as of 08:15, 15 May 2024

Solution Structure of the hSet2/HYPB SRI domain

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