Dr. Sudha Veeraraghavan, Assistant Professor

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Structural cell biology

Research in my lab addresses the molecular basis of cellular function, growth, and apoptosis. We use multinuclear multi-dimensional solution nuclear magnetic resonance (NMR) spectroscopy to elucidate the three-dimensional structures, binding interactions, and dynamics of proteins involved in critical cellular activities. DNA microarray technology is utilized to establish novel pathways and macromolecular interactions for structural studies. Structural information, together with biochemical data is used to gain insight into protein function.

Our investigations focus on proteins that regulate the cell cycle and/or those that are essential for organ development. The regulated expression of specific proteins in the cells of an embryo determine cellular fates and lead to normal development of an organism. The molecular basis for and the identities of all the macromolecules responsible for many of these events are unknown. Our interest in these cellular events has led us to investigate the structures of and interactions between proteins that (a) bind DNA, (b) regulate the cell cycle, and/or (c) are involved in tissue development. Current research focus in the laboratory inlcudes studies on the structural bases for the regulatory functions of angiogenic peptides and TEA domain transcription factors.

 

Selected publications and patents

Xia Y, Veeraraghavan S, Zhu Q, Gao X. (2008) Fast (4,3)D GFT-TS-NMR for NOESY of small to medium-sized proteins. J Mag Reson 190, 12-148.

Veeraraghavan S (2008) NMR spectroscopy and its value: A primer. Journal of Chemical Education 85 (4), 537-540

Yin S, Cabral F, Veeraraghavan S (2007) Amino Acid Substitutions at Proline 220 of β-Tubulin Confer Resistance to Paclitaxel and Colcemid. Molecular Cancer Therapeutics 6, 2798-2806.

Anbanandam, A., Albarado, D. C., Nguyen, C. T., Halder, G., Gao, X. and Veeraraghavan, S. Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain. Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17225-17230

Veeraraghavan, Sudha and Simons, Michael (2006) United States Patent, Serial Number 60/772,092. "Determinants of Function of Angiogenic Proline- and Arginine-Rich Peptides".

Wang Y, Veeraraghavan S, Cabral F. Related Articles, Links Intra-allelic suppression of a mutation that stabilizes microtubules and confers resistance to colcemid. Biochemistry. 2004 Jul 20; 43(28): 8965-73.

Xia Y, Zhu G, Veeraraghavan S, Gao X. Related Articles, Links (3,2)D GFT-NMR experiments for fast data collection from proteins. J Biomol NMR. 2004 Aug; 29(4):467-76.

3: Hari M, Wang Y, Veeraraghavan S, Cabral F. Related Articles, Links Mutations in alpha- and beta-tubulin that stabilize microtubules and confer resistance to colcemid and vinblastine. Mol Cancer Ther. 2003 Jul;2(7):597-605.

Sudha Veeraraghavan, Patricia A. Fagan, Haitao Hu, Vincent Lee, Jeffrey F. Harper, Bessie Huang, and Walter J. Chazin. Structural independence of the two EF-hand domains of caltractin. JBC 2002.

Veeraraghavan, S., Mello, C.C., Androphy, E.J., and Baleja, J.D. Structural correlates for enhanced stability in the E2 DNA-binding domain from bovine papillomaviruses. Biochemistry 38: 16115-16124, 1999.

Veeraraghavan, S., Mello, C.C., Lee, K.M., Androphy, E.J., and Baleja, J.D. 1H, 15N, and 13C NMR resonance assign-ments for the DNA-binding domain of the BPV-1 E2 protein. J. Biomol. NMR 11: 457-458, 1998.

Veeraraghavan, S., Baleja, J.D., and Gilbert, G.E. Structure and topography of the membrane-binding C2 domain of factor VIII in the presence of dodecylphosphocholine micelles. Biochem. J. 332: 549-555, 1998.

Veeraraghavan, S., Holzman, T. F., and Nall, B.T. Autocatalyzed protein folding. Biochemistry (accelerated publication) 35: 10601-10607, 1996.

Search PubMed for a complete list of Dr. Veeraraghavan's publications.