Regensburg 2013 – scientific programme

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BP: Fachverband Biologische Physik

BP 8: Posters: Proteins

BP 8.27: Poster

Monday, March 11, 2013, 17:30–19:30, Poster B2

Inhibition of HIV-1 protease: the rigidity perspective — •Jack Heal¹, Emilio Jimenez-Roldan^2,3, 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.