1xg1: Difference between revisions

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New page: left|200px<br /> <applet load="1xg1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xg1" /> '''Solution structure of Myb-domain of human T...
 
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[[Image:1xg1.gif|left|200px]]<br />
<applet load="1xg1" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1xg1" />
'''Solution structure of Myb-domain of human TRF2'''<br />


==About this Structure==
==Solution structure of Myb-domain of human TRF2==
1XG1 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=1XG1 OCA].  
<StructureSection load='1xg1' size='340' side='right'caption='[[1xg1]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xg1]] 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=1XG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XG1 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=1xg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xg1 OCA], [https://pdbe.org/1xg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xg1 RCSB], [https://www.ebi.ac.uk/pdbsum/1xg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xg1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TERF2_HUMAN TERF2_HUMAN] Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.<ref>PMID:9476899</ref> <ref>PMID:16166375</ref> <ref>PMID:20655466</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/xg/1xg1_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=1xg1 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Amiard, S.]]
[[Category: Amiard S]]
[[Category: Doudeau, M.]]
[[Category: Doudeau M]]
[[Category: Giraud-Panis, M.J.]]
[[Category: Giraud-Panis MJ]]
[[Category: Lancelot, G.]]
[[Category: Lancelot G]]
[[Category: Meudal, H.]]
[[Category: Meudal H]]
[[Category: Paoletti, J.]]
[[Category: Paoletti J]]
[[Category: Paquet, F.]]
[[Category: Paquet F]]
[[Category: helix-turn-helix]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:05:02 2007''

Latest revision as of 14:08, 9 May 2024

Solution structure of Myb-domain of human TRF2

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