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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pn3 OCA], [https://pdbe.org/2pn3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pn3 RCSB], [https://www.ebi.ac.uk/pdbsum/2pn3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pn3 ProSAT]</span></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=2pn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pn3 OCA], [https://pdbe.org/2pn3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pn3 RCSB], [https://www.ebi.ac.uk/pdbsum/2pn3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pn3 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The hepatitis C (HCV) internal ribosome entry site (IRES) element plays a central role in cap-independent translation of the viral genomic RNA. The unique conformation of IRES domain II is critical for 80S ribosomal assembly and initiation of viral translation. Here, the crystal structure of subdomain IIa of the HCV IRES has been determined at 2.3 A resolution, revealing the positions of divalent metal ions and complex inter-strand interactions that stabilize the L-shaped conformation of the RNA. The presence of divalent metal ions was necessary for crystal formation. Magnesium ions occupy specific sites that appear to be critical for the formation of the folded conformation. Subdomain IIa also was crystallized in the presence of strontium, which improved the diffraction quality of the crystals and the ability to identify interactions of the RNA with metal ions and tightly bound water molecules. The hinge region and noncanonical G-U base-pair motifs are stabilized by divalent metal ions and provide unique structural features that are potential interaction sites for small-molecule ligands. The information obtained from the crystal structure provides a basis for structure-guided design of HCV translation inhibitors targeting disruption of ribosomal assembly.
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| Structure of hepatitis C virus IRES subdomain IIa.,Zhao Q, Han Q, Kissinger CR, Hermann T, Thompson PA Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):436-43. Epub 2008, Mar 19. PMID:18391410<ref>PMID:18391410</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2pn3" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |