2rf2
From Proteopedia
(Difference between revisions)
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- | [[ | + | ==HIV reverse transcriptase in complex with inhibitor 7e (NNRTI)== |
+ | <StructureSection load='2rf2' size='340' side='right' caption='[[2rf2]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2rf2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hiv-1_m:b_hxb2r Hiv-1 m:b_hxb2r]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RF2 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MRX:5-BROMO-3-(PYRROLIDIN-1-YLSULFONYL)-1H-INDOLE-2-CARBOXAMIDE'>MRX</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11706 HIV-1 M:B_HXB2R])</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] </span></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rf2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rf2 RCSB], [http://www.ebi.ac.uk/pdbsum/2rf2 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/rf/2rf2_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 == | ||
+ | This Letter describes the design, synthesis, and biological evaluation of novel 3-indole sulfonamides as potent non-nucleoside reverse transcriptase inhibitors (NNRTIs) with balanced profiles against common HIV RT mutants K103N and Y181C. | ||
- | + | Novel indole-3-sulfonamides as potent HIV non-nucleoside reverse transcriptase inhibitors (NNRTIs).,Zhao Z, Wolkenberg SE, Sanderson PE, Lu M, Munshi V, Moyer G, Feng M, Carella AV, Ecto LT, Gabryelski LJ, Lai MT, Prasad SG, Yan Y, McGaughey GB, Miller MD, Lindsley CW, Hartman GD, Vacca JP, Williams TM Bioorg Med Chem Lett. 2008 Jan 15;18(2):554-9. Epub 2007 Nov 28. PMID:18083561<ref>PMID:18083561</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Reverse transcriptase|Reverse transcriptase]] | *[[Reverse transcriptase|Reverse transcriptase]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Hiv-1 m:b_hxb2r]] | [[Category: Hiv-1 m:b_hxb2r]] | ||
[[Category: RNA-directed DNA polymerase]] | [[Category: RNA-directed DNA polymerase]] |
Revision as of 09:15, 29 September 2014
HIV reverse transcriptase in complex with inhibitor 7e (NNRTI)
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Categories: Hiv-1 m:b hxb2r | RNA-directed DNA polymerase | Prasad, S. | Yan, Y. | Aid | Ai | Aspartyl protease | Capsid maturation | Core protein | Dna integration | Dna recombination | Dna-directed dna polymerase | Endonuclease | Hiv-1 revers transcriptase | Host-virus interaction | Hydrolase | Lipoprotein | Magnesium | Membrane | Metal-binding | Multifunctional enzyme | Myristate | Non-nucleoside inhibition | Nuclease | Nucleotidyltransferase | Nucleus | Phosphorylation | Protease | Rna-binding | Rna-directed dna polymerase | Transferase | Viral nucleoprotein | Virion | Zinc-finger