Crystal structures of inhibitor complexes of M PMV protease with visible flap loops

Mason Pfizer monkey virus protease PR was crystallized in complex with two pepstatin based inhibitors in P1 space group. In both crystal structures, the extended flap loops that lock the inhibitor substrate over the active site, are visible in the electron density either completely or with only small gaps, providing the first observation of the conformation of the flap loops in dimeric complex form of this retropepsin. The H bond network in the active site with D26N mutation differs from that reported for the P21 crystal structures and is similar to a rarely occurring system in HIV 1 P

Crystal structure of monomeric retroviral protease solved by protein folding game players

Following the failure of a wide range of attempts to solve the crystal structure of M-PMV retroviral protease by molecular replacement, we challenged players of the protein folding game Foldit to produce accurate models of the protein. Remarkably, Foldit players were able to generate models of sufficient quality for successful molecular replacement and subsequent structure determination. The refined structure provides new insights for the design of antiretroviral drugs

Crystal structure of a monomeric retroviral protease solved by protein folding game players

Following the failure of a wide range of attempts to solve the crystal structure of M-PMV retroviral protease by molecular replacement, we challenged players of the protein folding game Foldit to produce accurate models of the protein. Remarkably, Foldit players were able to generate models of sufficient quality for successful molecular replacement and subsequent structure determination. The refined structure provides new insights for the design of antiretroviral drugs