title: X-ray structure of HIV-1 protease tethered dimer complexed to ritonavir.
abstract: We report here the 2.5A structure of HIV-1 protease tethered-dimer ritonavir complex. The inhibitor bound in the active site has different conformations in the two orientations. There is only one hydrogen bond between the inhibitor and the enzyme. The conserved flap-water is not found in the present complex.
authors.affiliation: Solid State Physics Division, Bhabha Atomic Research Centre, Trombay, Mumbai-400085, India.
authors.forename: Amit
authors.initials: A
authors.lastname: Das
authors.forename: Dharmaraj Ramachandra
authors.initials: DR
authors.lastname: Rao
authors.forename: Madhusoodan Vijayacharya
authors.initials: MV
authors.lastname: Hosur
mesh_terms: D001665:Binding Sites; D018360:Crystallography, X-Ray / Q000379:methods; D016333:HIV Protease / Q000737:chemistry* / Q000378:metabolism; D017320:HIV Protease Inhibitors / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D019438:Ritonavir / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D017320:HIV Protease Inhibitors; D016333:HIV Protease; D019438:Ritonavir