3ou4 | pdb_00003ou4

MDR769 HIV-1 protease complexed with TF/PR hepta-peptide

spinqualitylabelsall models 3ou4, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ou4 is a 3 chain structure with sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3ots, 3oty, 3ou1, 3ou3, 3oua, 3oub, 3ouc, 3oud Gene: pol (Human immunodeficiency virus 1) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Under drug selection pressure, emerging mutations render HIV-1 protease drug resistant, leading to the therapy failure in anti-HIV treatment. It is known that nine substrate cleavage site peptides bind to wild type (WT) HIV-1 protease in a conserved pattern. However, how the multidrug-resistant (MDR) HIV-1 protease binds to the substrate cleavage site peptides is yet to be determined. MDR769 HIV-1 protease (resistant mutations at residues 10, 36, 46, 54, 62, 63, 71, 82, 84, and 90) was selected for present study to understand the binding to its natural substrates. MDR769 HIV-1 protease was co-crystallized with nine substrate cleavage site hepta-peptides. Crystallographic studies show that MDR769 HIV-1 protease has an expanded substrate envelope with wide open flaps. Furthermore, ligand binding energy calculations indicate weaker binding in MDR769 HIV-1 protease-substrate complexes. These results help in designing the next generation of HIV-1 protease inhibitors by targeting the MDR HIV-1 protease. Nine Crystal Structures Determine the Substrate Envelope of the MDR HIV-1 Protease.,Liu Z, Wang Y, Brunzelle J, Kovari IA, Kovari LC Protein J. 2011 Mar 12. PMID:21394574 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus protease

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