Lack of stereospecificity in the binding of the P2 amino acid of ritonavir to HIV protease
1997
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 A 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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