5yok: Difference between revisions

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-'''Unreleased structure'''
-The entry 5yok is ON HOLD  until Paper Publication
+==Structure of HIV-1 Protease in Complex with Inhibitor KNI-1657==
+<StructureSection load='5yok' size='340' side='right' caption='[[5yok]], [[Resolution|resolution]] 0.85&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5yok]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YOK FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8Z0:(4R)-N-[(2,6-dimethylphenyl)methyl]-3-[(2S,3S)-3-[[(2S)-2-[(7-methoxy-1-benzofuran-2-yl)carbonylamino]-2-[(3R)-oxolan-3-yl]ethanoyl]amino]-2-oxidanyl-4-phenyl-butanoyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxamide'>8Z0</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5yok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yok OCA], [http://pdbe.org/5yok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yok RCSB], [http://www.ebi.ac.uk/pdbsum/5yok PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yok ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The emergence of drug-resistant HIV from a widespread antiviral chemotherapy targeting HIV protease in the past decades is unavoidable and provides a challenge to develop alternative inhibitors. We synthesized a series of allophenylnorstatine-based peptidomimetics with various P3, P2, and P2 moieties. The derivatives with P2 tetrahydrofuranylglycine (Thfg) were found to be potent against wild type HIV-1 protease and the virus, leading to a highly potent compound 21f (KNI-1657) against lopinavir/ritonavir- or darunavir-resistant strains. Co-crystal structures of 21f and the wild-type protease revealed numerous key hydrogen bonding interactions with Thfg. These results suggest that the strategy to design allophenylnorstatine-based peptidomimetics combined with Thfg residue would be promising for generating candidates to overcome multidrug resistance.
-Authors: Adachi, M., Hidaka, K., Kuroki, R., Kiso, Y.
+Identification of Highly Potent Human Immunodeficiency Virus Type-1 Protease Inhibitors against Lopinavir and Darunavir Resistant Viruses from Allophenylnorstatine-Based Peptidomimetics with P2 Tetrahydrofuranylglycine.,Hidaka K, Kimura T, Sankaranarayanan R, Wang J, McDaniel KF, Kempf DJ, Kameoka M, Adachi M, Kuroki R, Nguyen JT, Hayashi Y, Kiso Y J Med Chem. 2018 Jun 28;61(12):5138-5153. doi: 10.1021/acs.jmedchem.7b01709. Epub, 2018 Jun 11. PMID:29852069<ref>PMID:29852069</ref>
-Description: Structure of HIV-1 Protease in Complex with Inhibitor KNI-1657
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5yok" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Adachi, M]]
+[[Category: Hidaka, K]]
 [[Category: Kiso, Y]]
 [[Category: Kuroki, R]]
-[[Category: Hidaka, K]]
+[[Category: Hydrolase]]
-[[Category: Adachi, M]]
+[[Category: Hydrolase-hydrolase inhibitor complex]]
+[[Category: Inhibitor]]