Considered a triumph in structure-based drug design, the development of the HIV-1 protease inhibitor class of drug has saved countless lives and inspired medicinal chemists throughout the world. These protease inhibitors were the first in a series of antiretroviral drugs which have made HIV infection a chronic condition for most patients in the developed world.

This crystal shows the HIV-1 protease enzyme complexed with the protease inhibitor indinavir. The protease is an essential component of the HIV-1 life cycle. It chops up the protein chain created by the HIV virus into its functional peptide units. The timing of this proteolysis must be precisely controlled, making inhibition of the protease an excellent drug target.

The protease enzyme is small and made up of 2 protein chains each only about 100 amino acids long. The 2 chains form a tunnel with 2 protein flaps. The flaps can open and accomodate the nascent HIV-1 peptide tightly in the long tunnel. The active site for peptide cleavage is located inside the tunnel. In this crystal, indinavir can be seen bound within the tunnel, blocking access to the active site.

$79.95 $69.95