2l88
From Proteopedia
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==Solution structure of all parallel G-quadruplex formed by the oncogene RET promoter sequence== | ==Solution structure of all parallel G-quadruplex formed by the oncogene RET promoter sequence== | ||
| - | <StructureSection load='2l88' size='340' side='right' caption='[[2l88 | + | <StructureSection load='2l88' size='340' side='right'caption='[[2l88]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[2l88]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L88 OCA]. < | + | <table><tr><td colspan='2'>[[2l88]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L88 FirstGlance]. <br> |
| - | <b> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <b> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l88 OCA], [https://pdbe.org/2l88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l88 RCSB], [https://www.ebi.ac.uk/pdbsum/2l88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l88 ProSAT]</span></td></tr> |
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
RET protein functions as a receptor-type tyrosine kinase and has been found to be aberrantly expressed in a wide range of human diseases. A highly GC-rich region upstream of the promoter plays an important role in the transcriptional regulation of RET. Here, we report the NMR solution structure of the major intramolecular G-quadruplex formed on the G-rich strand of this region in K(+) solution. The overall G-quadruplex is composed of three stacked G-tetrad and four syn guanines, which shows distinct features for all parallel-stranded folding topology. The core structure contains one G-tetrad with all syn guanines and two other with all anti-guanines. There are three double-chain reversal loops: the first and the third loops are made of 3 nt G-C-G segments, while the second one contains only 1 nt C10. These loops interact with the core G-tetrads in a specific way that defines and stabilizes the overall G-quadruplex structure and their conformations are in accord with the experimental mutations. The distinct RET promoter G-quadruplex structure suggests that it can be specifically involved in gene regulation and can be an attractive target for pathway-specific drug design. | RET protein functions as a receptor-type tyrosine kinase and has been found to be aberrantly expressed in a wide range of human diseases. A highly GC-rich region upstream of the promoter plays an important role in the transcriptional regulation of RET. Here, we report the NMR solution structure of the major intramolecular G-quadruplex formed on the G-rich strand of this region in K(+) solution. The overall G-quadruplex is composed of three stacked G-tetrad and four syn guanines, which shows distinct features for all parallel-stranded folding topology. The core structure contains one G-tetrad with all syn guanines and two other with all anti-guanines. There are three double-chain reversal loops: the first and the third loops are made of 3 nt G-C-G segments, while the second one contains only 1 nt C10. These loops interact with the core G-tetrads in a specific way that defines and stabilizes the overall G-quadruplex structure and their conformations are in accord with the experimental mutations. The distinct RET promoter G-quadruplex structure suggests that it can be specifically involved in gene regulation and can be an attractive target for pathway-specific drug design. | ||
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Solution structure of all parallel G-quadruplex formed by the oncogene RET promoter sequence.,Tong X, Lan W, Zhang X, Wu H, Liu M, Cao C Nucleic Acids Res. 2011 May 2. PMID:21540209<ref>PMID:21540209</ref> | Solution structure of all parallel G-quadruplex formed by the oncogene RET promoter sequence.,Tong X, Lan W, Zhang X, Wu H, Liu M, Cao C Nucleic Acids Res. 2011 May 2. PMID:21540209<ref>PMID:21540209</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 2l88" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Synthetic construct]] |
| - | [[Category: | + | [[Category: Cao C]] |
| - | [[Category: | + | [[Category: Tong X]] |
| - | + | ||
Current revision
Solution structure of all parallel G-quadruplex formed by the oncogene RET promoter sequence
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