title: Virtual screening of HIV-1 protease inhibitors against human cytomegalovirus protease using docking and molecular dynamics.
abstract: The clearance of cytomegalovirus viraemia in HIV-1-infected patients may partly result from the inhibition of cytomegalovirus protease by HIV-1 protease inhibitors contained in highly active antiretroviral therapy. We used a computational method to calculate the binding affinity of six HIV-1 protease inhibitors to cytomegalovirus protease based on its X-ray crystallography structure. The calculations showed that amprenavir and indinavir occupy the substrate-binding site of the cytomegalovirus protease with high affinity, and may be implicated in alleviating cytomegalovirus infection.
authors.affiliation: Department of Microbiology, University of Washington School of Medicine, Seattle, WA 98195, USA.
authors.forename: Ekachai
authors.initials: E
authors.lastname: Jenwitheesuk
authors.forename: Ram
authors.initials: R
authors.lastname: Samudrala
mesh_terms: D017088:AIDS-Related Opportunistic Infections / Q000378:metabolism / Q000821:virology; D023241:Antiretroviral Therapy, Highly Active / Q000379:methods; D001665:Binding Sites; D002219:Carbamates; D018360:Crystallography, X-Ray / Q000379:methods; D003587:Cytomegalovirus / Q000201:enzymology*; D003586:Cytomegalovirus Infections / Q000378:metabolism / Q000821:virology; D005663:Furans; D015658:HIV Infections / Q000188:drug therapy / Q000378:metabolism; D017320:HIV Protease Inhibitors / Q000378:metabolism*; D015497:HIV-1; D006801:Humans; D019469:Indinavir / Q000378:metabolism; D015394:Molecular Structure; D010447:Peptide Hydrolases / Q000378:metabolism*; D013449:Sulfonamides / Q000378:metabolism
chemical_list: D002219:Carbamates; D005663:Furans; D017320:HIV Protease Inhibitors; D013449:Sulfonamides; C095108:amprenavir; D019469:Indinavir; D010447:Peptide Hydrolases