High-resolution structure of a retroviral protease folded as a monomer

Acta Cryst. (2011). D67, 907-914 (http://doi.org/g3h)

Comparison of electrostatic potential surfaces of retroviral protease monomer (left) and a subunit extracted from a dimeric molecule (right).

Although retroviral protease, which is a homodimeric enzyme, has been the subject of numerous studies, the structure of its protomeric subunit has defied crystallographers for a long time. Finally, a suitable molecular replacement model has been created by players of the online protein folding game, Foldit. The crystal structure of monomeric protease from an HIV-like monkey virus shows a molecule with a canonical core but with novel conformation of some key elements, e.g. the 'flap'. This new information can be used to design novel antiretroviral drugs.