Solution studies of hpv-16 E2c, its DNA binding site and the complex.

NADRA, A., ELISEO, T., MORINO, V., TROTTA, E., FERREIRO, D.U., PACI, M., PRAT GAY, G. DE AND CICERO, D.

Iguazu, Argentina.

Congreso; XL Congreso de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB); 2004

SAIB

SOLUTION STUDIES OF HPV-16 E2C, ITS DNA BINDING SITE AND THE COMPLEX Alejandro D. Nadra‡, Tommaso Eliseo†, Valentina Morino†, Edoardo Trotta†, Diego U. Ferreiro‡, Maurizio Paci†, Gonzalo de Prat-Gay‡ and Daniel O. Cicero† ‡ Instituto Leloir - Instituto de Investigaciones Bioquímicas, FCEyN-UBA and CONICET, Argentina. †Dipartimento di Chimica, Università di Roma “Tor Vergata”, Rome, Italy. E-mail: anadra@leloir.org.ar Papillomaviruses are DNA viruses that infect a wide range of mammals, and represent a serious health threat for humans. Gene transcription in papillomavirus is regulated by the E2 protein which has several binding sites. These have different affinities and their occupancy varies along viral cycle. We are interested in the DNA recognition mechanism of E2C, both as a means to understand its role in papillomavirus gene regulation and as a model for protein-DNA recognition. With these goals in mind, we tackled a thorough investigation of the structural plasticity of HPV-16 E2C by multidimensional NMR. We also compare this data with those of the bound protein. Finally, we present conformational differences between two binding sites for which E2 shows different affinity. The overall analysis of this data provides a picture of the structural plasticity of this protein and its binding sites in solution.