Abstract
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 Å difference in the backbone that allows the valine side chain of both compounds to project into the S2 subsite of the enzyme.
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