Lack of stereospecificity in the binding of the P2 amino acid of ritonavir to HIV protease

✍ Scribed by Dale J. Kempf; Akhteruzzaman Molla; Kennan C. Marsh; Chang Park; A.David Rodrigues; Marina Korneyeva; Sudthida Vasavanonda; Edith McDonald; Charles A. Flentge; Steven Muchmore; Norman E. Wideburg; Ayda Saldivar; Art Cooper; Warren M. Kati; Kent D. Stewart; Daniel W. Norbeck

• Book ID: 104364893
• Publisher: Elsevier Science
• Year: 1997
• Tongue: English
• Weight: 305 KB
• Volume: 7
• Category: Article
• ISSN: 0960-894X
• DOI: 10.1016/s0960-894x(97)00080-2

✦ Synopsis

The biological and pharmacokinetic properties of the HIV protease inhibitor ritonavir and its D-valinyl diastereomer, A-117673, were found to be indistinguishable. The X-ray crystal structure of the A-117673/HIV protease complex demonstrated similar binding modes for the two inhibitors, with a ca 1 /k difference in the backbone that allows the valine side chain of both compounds to project into the $2 subsite of the enzyme.