5yok | pdb_00005yok

Structure of HIV-1 Protease in Complex with Inhibitor KNI-1657

spinqualitylabelsall models 5yok, resolution 0.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5yok is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 8Z0, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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