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2l3n

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Solution structure of Rap1-Taz1 fusion protein

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Retrieved from "http://52.214.119.220/wiki/index.php/2l3n"

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 ==Solution structure of Rap1-Taz1 fusion protein==
-<StructureSection load='2l3n' size='340' side='right'caption='[[2l3n]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2l3n' size='340' side='right'caption='[[2l3n]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l3n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L3N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l3n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L3N FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">taz1, myb, myb1, SPAC16A10.07c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</td></tr>
+</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=2l3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l3n OCA], [https://pdbe.org/2l3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l3n RCSB], [https://www.ebi.ac.uk/pdbsum/2l3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l3n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/RAP1_SCHPO RAP1_SCHPO]] Involved in the regulation of telomere length, clustering and has a specific role in telomere position effect (TPE). Unlike yeast, exhibits no effect in transcription regulation.<ref>PMID:11676924</ref> <ref>PMID:11676925</ref> <ref>PMID:19948484</ref>
+[https://www.uniprot.org/uniprot/TAZ1_SCHPO TAZ1_SCHPO] Regulates telomere length and function. Required for the repression of telomere-adjacent gene expression and for normal meiosis or sporulation. It may be a negative regulator of the telomere-replicating enzyme, telomerase, or may protect against activation of telomerase-independent pathways of telomere elongation. It may be involved in the interactions between chromosomes and spindle proteins, disruption of these interactions would lead to defective meiosis.[https://www.uniprot.org/uniprot/RAP1_SCHPO RAP1_SCHPO] Involved in the regulation of telomere length, clustering and has a specific role in telomere position effect (TPE). Unlike yeast, exhibits no effect in transcription regulation.<ref>PMID:11676924</ref> <ref>PMID:11676925</ref> <ref>PMID:19948484</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Repressor activator protein 1 (RAP1) is the most highly conserved telomere protein. It is involved in protecting chromosome ends in fission yeast and promoting gene silencing in Saccharomyces cerevisiae, whereas it represses homology-directed recombination at telomeres in mammals. To understand how RAP1 has such diverse functions at telomeres, we solved the crystal or solution structures of the RAP1 C-terminal (RCT) domains of RAP1 from multiple organisms in complex with their respective protein-binding partners. Our analysis establishes RAP1(RCT) as an evolutionarily conserved protein-protein interaction module. In mammalian and fission yeast cells, this module interacts with TRF2 and Taz1, respectively, targeting RAP1 to chromosome ends for telomere protection. In contrast, S. cerevisiae RAP1 uses its RCT domain to recruit Sir3 to telomeres to mediate gene silencing. Together, our results show that, depending on the organism, the evolutionarily conserved RAP1 RCT motif has diverse functional roles at telomeres.
-A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms.,Chen Y, Rai R, Zhou ZR, Kanoh J, Ribeyre C, Yang Y, Zheng H, Damay P, Wang F, Tsujii H, Hiraoka Y, Shore D, Hu HY, Chang S, Lei M Nat Struct Mol Biol. 2011 Jan 9. PMID:21217703<ref>PMID:21217703</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2l3n" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Fission yeast]]
 [[Category: Large Structures]]
-[[Category: Chen, Y]]
+[[Category: Schizosaccharomyces pombe 972h-]]
-[[Category: Hu, H]]
+[[Category: Chen Y]]
-[[Category: Lei, M]]
+[[Category: Hu H]]
-[[Category: Wang, F]]
+[[Category: Lei M]]
-[[Category: Zhou, Z R]]
+[[Category: Wang F]]
-[[Category: Dna binding protein]]
+[[Category: Zhou ZR]]
-[[Category: Rap1]]
-[[Category: Taz1]]

2l3n

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Solution structure of Rap1-Taz1 fusion protein

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