3nj7
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3nj7 is ON HOLD Authors: Kiliszek, A., Kierzek, R., Krzyzosiak, W.J., Rypniewski, W. Description: 1.9 A resolution X-ray structure of (GGCAGCAGCC)2...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==1.9 A resolution X-ray structure of (GGCAGCAGCC)2== | |
| + | <StructureSection load='3nj7' size='340' side='right'caption='[[3nj7]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3nj7]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NJ7 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]] 1.904Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3nj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nj7 OCA], [https://pdbe.org/3nj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nj7 RCSB], [https://www.ebi.ac.uk/pdbsum/3nj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nj7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | CAG repeats occur predominantly in the coding regions of human genes, which suggests their functional importance. In some genes, these sequences can undergo pathogenic expansions leading to neurodegenerative polyglutamine (poly-Q) diseases. The mutant transcripts containing expanded CAG repeats possibly contribute to pathogenesis in addition to the well-known pathogenic effects of mutant proteins. We have analysed two crystal forms of RNA duplexes containing CAG repeats: (GGCAGCAGCC)(2). One of the structures has been determined at atomic resolution (0.95 A) and the other at 1.9 A. The duplexes include non-canonical A-A pairs that fit remarkably well within a regular A-helix. All the adenosines are in the anti-conformation and the only interaction within each A-A pair is a single C2-H2...N1 hydrogen bond. Both adenosines in each A-A pair are shifted towards the major groove, although to different extents; the A which is the H-bond donor stands out more (the 'thumbs-up' conformation). The main effect on the helix conformation is a local unwinding. The CAG repeats and the previously examined CUG structures share a similar pattern of electrostatic charge distribution in the minor groove, which could explain their affinity for the pathogenesis-related MBNL1 protein. | ||
| - | + | Atomic resolution structure of CAG RNA repeats: structural insights and implications for the trinucleotide repeat expansion diseases.,Kiliszek A, Kierzek R, Krzyzosiak WJ, Rypniewski W Nucleic Acids Res. 2010 Aug 11. PMID:20702420<ref>PMID:20702420</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3nj7" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kierzek R]] | ||
| + | [[Category: Kiliszek A]] | ||
| + | [[Category: Krzyzosiak WJ]] | ||
| + | [[Category: Rypniewski W]] | ||
Current revision
1.9 A resolution X-ray structure of (GGCAGCAGCC)2
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