Ph.D., 2000, Rockefeller University

Biophysical Chemistry

Crystallographic studies of hepatitis C viral proteins

Our laboratory focuses on characterizing the structure and function of many of the HCV proteins and important cellular factors. We have determined the structure of two essential HCV proteins (NS2 and NS5A) by X-ray crystallography. The information gleaned from these studies was used to further define the function of these proteins. A better understand of the structure and function of the HCV proteins will contribute greatly to the current knowledge of HCV biology and aid in the design of novel therapies to combat HCV infection.

Lorenz IC, Marcotrigiano J, Dentzer TG, Rice CM. (2006) Structure of the catalytic domain of the hepatitis C virus NS2-3 protease. Nature 442:831-5 Tellinghuisen TL, Marcotrigiano J, Rice CM. (2005) Structure of the zinc-binding domain of an essential replicase component of hepatitis C. Nature 435:374-9 Tellinghuisen TL, Marcotrigiano J, Gorbalenya AE, Rice CM. (2004) The NS5A protein of hepatitis C virus is a zinc metalloprotein. JBC 279:48576-87 Marcotrigiano J, Lomakin I, Pestova T, Sonenberg N, Hellen CUT, Burley SK. (2000) A conserved HEAT domain within elF4G directs assembly of the translation initiation machinery. Molecular Cell 7:193-203 Marcotrigiano J, Gingras A-C, Sonenberg N, Burley SK. (1999) Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of elF4G. Molecular Cell 3:707-16 Marcotrigiano J, Gingras A-C, Sonenberg N, Burley SK. (1997) Cocrystal structure of the messanger RNA 5' cap-binding protein (elF4E) bound to 7-methyl-GDP. Cell 89:951-61