X-ray structure of HIV-1 protease tethered dimer complexed to ritonavir.
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.
Das
Amit
A
Solid State Physics Division, Bhabha Atomic Research Centre, Trombay, Mumbai-400085, India.
Rao
Dharmaraj Ramachandra
DR
Hosur
Madhusoodan Vijayacharya
MV
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
D017320:HIV Protease Inhibitors; D016333:HIV Protease; D019438:Ritonavir