3lkz
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase== | |
| - | + | <StructureSection load='3lkz' size='340' side='right' caption='[[3lkz]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3lkz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/West_nile_virus West nile virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LKZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LKZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oy0|2oy0]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Non-structural protein 5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11082 West Nile virus])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lkz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lkz RCSB], [http://www.ebi.ac.uk/pdbsum/3lkz PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lk/3lkz_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The flavivirus methyltransferase (MTase) sequentially methylates the N7 and 2'-O positions of the viral RNA cap (GpppA-RNA --> m(7)GpppA-RNA --> m(7)GpppAm-RNA), using S-adenosyl-l-methionine (AdoMet) as a methyl donor. We report here that sinefungin (SIN), an AdoMet analog, inhibits several flaviviruses through suppression of viral MTase. The crystal structure of West Nile virus MTase in complex with SIN inhibitor at 2.0-A resolution revealed a flavivirus-conserved hydrophobic pocket located next to the AdoMet-binding site. The pocket is functionally critical in the viral replication and cap methylations. In addition, the N7 methylation efficiency was found to correlate with the viral replication ability. Thus, SIN analogs with modifications that interact with the hydrophobic pocket are potential specific inhibitors of flavivirus MTase. | ||
| - | + | Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase.,Dong H, Liu L, Zou G, Zhao Y, Li Z, Lim SP, Shi PY, Li H J Biol Chem. 2010 Oct 15;285(42):32586-95. Epub 2010 Aug 4. PMID:20685660<ref>PMID:20685660</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: West nile virus]] | [[Category: West nile virus]] | ||
| - | [[Category: Li, H M | + | [[Category: Li, H M]] |
| - | [[Category: Liu, L H | + | [[Category: Liu, L H]] |
[[Category: Flavivirus]] | [[Category: Flavivirus]] | ||
[[Category: Inhibitor]] | [[Category: Inhibitor]] | ||
| Line 18: | Line 40: | ||
[[Category: Rna replication]] | [[Category: Rna replication]] | ||
[[Category: Viral protein]] | [[Category: Viral protein]] | ||
| - | [[Category: West nile virus]] | ||
Revision as of 14:56, 18 December 2014
Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase
| |||||||||||
