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Xiang Xu

Published on 4/23/2019

Xiang Xu


Xiang Xu, Ph.D., M.D. 

Research Fellow

Beth Israel Deaconess Medical Center

Harvard Medical School

330 Brookline Ave

E/CLS Room 924

Boston MA, 02215

Phone: (617)735-4032  Fax: (617)735-1234



Xu, X., Liu, Y., Weiss, S., Arnold, E., Sarafianos, S.G., and Ding, J. “Molecular model of SARS coronavirus polymerase: implications for biochemical functions and drug design” Nucleic Acids Research, Dec 15; 31(24):7117-30 (2003).

Yu, Y., Liu, Y., Shen, N., Xu, X., Jia, J., Jin, Y., Arnold, E., and Ding, J.* “Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding and angiogenesis activity” Journal of Biological Chemistry, Feb 27; 279(9):8378-88 (2004).

Xu, X., Zhao, J., Xu, Z., Peng, B., Huang, Q., Arnold, E., and Ding, J.* “Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity” Journal of Biological Chemistry, Aug 6;279(32):33946-57 (2004).

Yu, Y., Li, S., Xu, X., Li, Y., Guan, K., Arnold, E., Ding, J.  “Structural basis for the unique biological function of small GTPase Rheb” Journal of Biological Chemistry, Apr 29; 280(17):17093-17100 (2005) 

Ding, J., Yu, Y., Li, S., Xu, X.  “Structure of small GTPase human Rheb provides a structural basis for its unique biological function and reveals a novel GTP hydrolysis mechanism” Acta Cryst. (2005). A61, C196 

Wang, Y., Xu, X., Luo, C., Ma, Z., Jiang, H., Ding, J., Wen, Y. “Mutational analysis revealed that conservation of hepatitis B virus reverse transcriptase residue 306 (rtP306) is crucial for encapsidation of pregenomic  RNA” FEBS Letters, Feb 6; 581(3):558-564(2007) 

Wang, Y., Xu, X., Luo, C., Ma, Z., Jiang, H., Ding, J., Wen, Y. “A putative new Domain target for anti-hepatitis B virus: residues flanking hepatitis B virus reverse transcriptase residue 306 (rtP306)” Journal of Medical Virology, Jun; 79(6):676-682(2007) 

Research Interests

I study the structure and function of proteins, and protein-protein interactions, that play important roles in mammalian biology, human health, and disease. I primarily explore molecular and mechanistic questions pertaining to cell surface receptor recognition and signaling transduction in the cancer development, virus infection and thrombosis formation. By using such information, we can make rational structure-based drug design against many health-threaten diseases. I seek to understand how these molecular events coordinate with the higher order physiology of the cell.