3bua

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{{Seed}}
 
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[[Image:3bua.png|left|200px]]
 
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==Crystal Structure of TRF2 TRFH domain and APOLLO peptide complex==
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The line below this paragraph, containing "STRUCTURE_3bua", creates the "Structure Box" on the page.
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<StructureSection load='3bua' size='340' side='right'caption='[[3bua]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3bua]] is a 8 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=3BUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BUA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.5&#8491;</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=3bua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bua OCA], [https://pdbe.org/3bua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bua RCSB], [https://www.ebi.ac.uk/pdbsum/3bua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bua ProSAT]</span></td></tr>
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{{STRUCTURE_3bua| PDB=3bua | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|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/bu/3bua_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/main_output.php?pdb_ID=3bua ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mammalian telomeres are protected by a six-protein complex, shelterin. Shelterin contains two closely related proteins, TRF1 and TRF2, which recruit various proteins to telomeres. Here we dissect the interactions of TRF1 and TRF2 with their shared binding partner, TIN2, and other shelterin accessory factors. TRF1 recognizes TIN2 using a conserved molecular surface in its TRF homology (TRFH) domain. However, this same surface does not act as a TIN2 binding site in TRF2, and TIN2 binding to TRF2 is mediated by a region outside the TRFH domain. Instead, the TRFH docking site of TRF2 binds a shelterin accessory factor Apollo, which does not interact with the TRFH domain of TRF1. Conversely, the TRFH domain of TRF1, but not of TRF2, interacts with another shelterin associated factor PinX1.
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===Crystal Structure of TRF2 TRFH domain and APOLLO peptide complex===
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A Shared Docking Motif in TRF1 and TRF2 Used for Differential Recruitment of Telomeric Proteins.,Chen Y, Yang Y, van Overbeek M, Donigian JR, Baciu P, de Lange T, Lei M Science. 2008 Jan 17;. PMID:18202258<ref>PMID:18202258</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_18202258}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3bua" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18202258 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18202258}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3BUA is a 8 chains structure of sequences 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=3BUA OCA].
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==Reference==
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<ref group="xtra">PMID:18202258</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Baciu, P.]]
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[[Category: Large Structures]]
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[[Category: Chen, Y.]]
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[[Category: Baciu P]]
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[[Category: Donigian, J R.]]
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[[Category: Chen Y]]
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[[Category: Lange, T de.]]
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[[Category: Donigian JR]]
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[[Category: Lei, M.]]
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[[Category: Lei M]]
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[[Category: Overbeek, M van.]]
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[[Category: Yang Y]]
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[[Category: Yang, Y.]]
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[[Category: De Lange T]]
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[[Category: Alternative splicing]]
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[[Category: Van Overbeek M]]
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[[Category: Cell cycle]]
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[[Category: Chromosomal protein]]
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[[Category: Dna binding protein]]
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[[Category: Dna damage]]
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[[Category: Dna repair]]
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[[Category: Dna-binding]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Polymorphism]]
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[[Category: Telomere]]
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[[Category: Trf2 trfh domain dimerization domain apollo peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:53:44 2009''
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Current revision

Crystal Structure of TRF2 TRFH domain and APOLLO peptide complex

PDB ID 3bua

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