4rqi
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4rqi is ON HOLD Authors: Miron, S., Guimaraes, B., Gaullier, G., Giraud-Panis, M.-J., Gilson, E., Le Du, M.-H. Description: Structure of TRF2/RAP1 ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of TRF2/RAP1 secondary interaction binding site== | |
| - | + | <StructureSection load='4rqi' size='340' side='right'caption='[[4rqi]], [[Resolution|resolution]] 2.44Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4rqi]] 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=4RQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RQI FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4405Å</td></tr> | |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4rqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rqi OCA], [https://pdbe.org/4rqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rqi RCSB], [https://www.ebi.ac.uk/pdbsum/4rqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rqi 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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gaullier G]] | ||
| + | [[Category: Gilson E]] | ||
| + | [[Category: Giraud-Panis M-J]] | ||
| + | [[Category: Guimaraes B]] | ||
| + | [[Category: Le Du M-H]] | ||
| + | [[Category: Miron S]] | ||
Current revision
Structure of TRF2/RAP1 secondary interaction binding site
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