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3k6g
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3k6g is ON HOLD Authors: Chen, Y., Rai, R., Yang, Y.T., Zheng, H., Chang, S., Lei, M. Description: Crystal structure of Rap1 and TRF2 complex ''Pa...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Rap1 and TRF2 complex== | |
| - | + | <StructureSection load='3k6g' size='340' side='right'caption='[[3k6g]], [[Resolution|resolution]] 1.95Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3k6g]] is a 6 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=3K6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K6G 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]] 1.95Å</td></tr> | |
| - | + | <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> | |
| - | '' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6g OCA], [https://pdbe.org/3k6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k6g RCSB], [https://www.ebi.ac.uk/pdbsum/3k6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k6g ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TE2IP_HUMAN TE2IP_HUMAN] Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes.<ref>PMID:16166375</ref> <ref>PMID:19763083</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chang S]] | ||
| + | [[Category: Chen Y]] | ||
| + | [[Category: Lei M]] | ||
| + | [[Category: Rai R]] | ||
| + | [[Category: Yang YT]] | ||
| + | [[Category: Zheng H]] | ||
Current revision
Crystal structure of Rap1 and TRF2 complex
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Categories: Homo sapiens | Large Structures | Chang S | Chen Y | Lei M | Rai R | Yang YT | Zheng H
