Regensburg 2013 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 8: Posters: Proteins
BP 8.27: Poster
Montag, 11. März 2013, 17:30–19:30, Poster B2
Inhibition of HIV-1 protease: the rigidity perspective — •Jack Heal1, Emilio Jimenez-Roldan2,3, Stephen Wells2, Robert Freedman3, and Rudolph Römer2 — 1MOAC Doctoral Training Center, University of Warwick, Coventry, UK, CV4 7AL — 2Department of Physics, University of Warwick, Coventry, UK, CV4 7AL — 3Department of Life Sciences, University of Warwick, Coventry, UK, CV4 7AL
HIV-1 protease is a key drug target due to its role in the life-cycle of the HIV-1 virus. There are more than 200 high resolution (≤ 2 Å) X-ray crystal structures of the enzyme in complex with a variety of ligands. We have carried out a broad study of these structures using the rigidity analysis software FIRST. This approach allows us to make inferences about the effect of ligand binding upon the rigidity of the protein. The protease inhibitors currently used as part of antiretroviral treatments can be split into two categories, which may offer an explanation for the efficacy of particular combination therapies.