3l82

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==X-ray Crystal structure of TRF1 and Fbx4 complex==
==X-ray Crystal structure of TRF1 and Fbx4 complex==
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<StructureSection load='3l82' size='340' side='right' caption='[[3l82]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='3l82' size='340' side='right'caption='[[3l82]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3l82]] is a 2 chain structure with sequence 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=3L82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L82 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3l82]] 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=3L82 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L82 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TERF1, PIN2, TRBF1, TRF, TRF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), FBXO4, FBX4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3l82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l82 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l82 RCSB], [http://www.ebi.ac.uk/pdbsum/3l82 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3l82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l82 OCA], [https://pdbe.org/3l82 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l82 RCSB], [https://www.ebi.ac.uk/pdbsum/3l82 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l82 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TERF1_HUMAN TERF1_HUMAN]] Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG 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.<ref>PMID:16166375</ref> [[http://www.uniprot.org/uniprot/FBX4_HUMAN FBX4_HUMAN]] Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes ubiquitination of CCND1 and its subsequent proteasomal degradation. Recognizes TERF1 and promotes its ubiquitination together with UBE2D1.<ref>PMID:10531035</ref> <ref>PMID:16275645</ref> <ref>PMID:18598945</ref> <ref>PMID:20159592</ref> <ref>PMID:20181953</ref>
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[https://www.uniprot.org/uniprot/TERF1_HUMAN TERF1_HUMAN] Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG 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.<ref>PMID:16166375</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l8/3l82_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l8/3l82_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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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</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=3l82 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3l82" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Chen, Y]]
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[[Category: Large Structures]]
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[[Category: Diehl, J A]]
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[[Category: Chen Y]]
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[[Category: Lei, M]]
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[[Category: Diehl JA]]
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[[Category: Liu, X D]]
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[[Category: Lei M]]
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[[Category: Wang, W]]
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[[Category: Liu XD]]
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[[Category: Yang, X M]]
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[[Category: Wang W]]
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[[Category: Yang, Y T]]
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[[Category: Yang XM]]
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[[Category: Zeng, Z X]]
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[[Category: Yang YT]]
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[[Category: Adp-ribosylation]]
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[[Category: Zeng ZX]]
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[[Category: Cell cycle]]
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[[Category: Cell division]]
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[[Category: Chromosomal protein]]
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[[Category: Cytoskeleton]]
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[[Category: Dna-binding]]
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[[Category: Gtpase domain]]
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[[Category: Helix]]
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[[Category: Mitosis]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Telomere]]
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[[Category: Trfh domain]]
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[[Category: Ubl conjugation pathway]]
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Current revision

X-ray Crystal structure of TRF1 and Fbx4 complex

PDB ID 3l82

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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