Liang Tong

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Biophysics and Biophysical Chemistry Program

Please see my Research Summary for more detailed information on materials discussed here.

A major focus of my current research is on enzymes that are involved in the biosynthesis and metabolism of fatty acids. These include acetyl-coenzyme A carboxylase (ACC), carnitine acyltransferase, malic enzyme (ME) and others. These enzymes play crucial roles in the synthesis and oxidation of long-chain fatty acids, and are important targets for drug development against obesity, diabetes and other human diseases.

Another area of my research is on elucidating the molecular basis for signal transduction by receptors that play crucial roles in innate immunity and host defense. We are currently studying two families of receptors that are important for host defense - the Toll-like receptors (TLRs) and the interleukin-1 receptor superfamily (IL-1Rs).

Additional projects in the laboratory include enzymes and proteins of biological and medical importance. For example, structural biology techniques will be used to study the catalytic mechanism of the protease of human cytomegalovirus, a serious pathogen afflicting AIDS patients, organ transplant recipients and newborns.

Finally, I will continue my interest in the development of new techniques and computer programs for macromolecular crystallography

Zhang H, Yang Z, Shen Y, L. Tong. Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase. Science. 2003 Mar 28;299(5615):2064-7.

Jogl G, L. Tong. Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport. Cell. 2003 Jan 10;112(1):113-22

Z. Yang, C.W. Lanks, L. Tong. Molecular mechanism for the regulation of human mitochondrial NAD(P)+-dependent malic enzyme by ATP and fumarate. Structure (2002). 10, 951-960.

C. Pargellis, L. Tong, L. Churchill, P.F. Cirillo, T. Gilmore, A.G. Graham, P.M. Grob, E.R. Hickey, N. Moss, S. Pav, J. Regan. Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Nature Struct. Biol. (2002). 9, 268-272.

Batra R, Khayat R, L. Tong. Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease. Nat Struct Biol. (2001) Sep;8(9):810-7.

Jogl G, Tao X, Xu Y, L. Tong. COMO: a program for combined molecular replacement. Acta Crystallogr D Biol Crystallogr. (2001) Aug;57(Pt 8):1127-34.

Khayat R, Batra R, Massariol MJ, Lagace L, L. Tong.  Investigating the role of histidine 157 in the catalytic activity of human cytomegalovirus protease. Biochemistry. (2001) May 29;40(21):6344-51.

Y. Xu, X. Tao, B. Shen, T. Horng, R. Medzhitov, J.L. Manley, L. Tong. (2000). Structural basis for signal transduction by the Toll/interleukin-1 receptor domains. Nature, 408, 111-115.

Z. Yang, D.L. Floyd, G. Loeber & L. Tong. Structure of a closed form of human malic enzyme and implications for catalytic mechanism. Nature Struct. Biol. 7, 251-257, (2000).