IUCr journals

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

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

[Potential surfaces] 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.

M. Gilski, M. Kazmierczyk, S. Krzywda, H. Zábranská, S. Cooper, Z. Popovic, F. Khatib, F. DiMaio, J. Thompson, D. Baker, I. Pichová and M. Jaskolski