Melanie Cocco
Molecular Biology & Biochemistry, School of Biological Sciences
Phone: (949) 824-4487
Email: mcocco@uci.edu
Cocco Lab
http://www.faculty.uci.edu/profile.cfm?faculty_id=4947
Melanie Cocco
Dr. Cocco uses nuclear magnetic resonance (NMR) and other biophysical techniques to study DNA binding proteins. Their research has applications in understanding cancer mechanisms at the molecular level.
One of those DNA binding proteins is p53, a known tumor suppressor. Many cancers can be traced to a set of several individual point mutations in this protein that result in destabilization of the structure. Several p53 rescue mutations have been identified that cancel the effect of a cancerous mutation by restoring stability and function. Their goal is to establish the mechanism through which these rescue mutations stabilize the structure through NMR dynamics measurements and use this knowledge for intelligent drug design of small molecules that can mimic this mechanism. Other DNA-binding proteins of interest include a bypass polymerase and CytR, a bacterial transcription factor.
Selected Publications:
Tretyachenko-Ladokhina, V., Cocco, M. J., and Senear, D. F. (2006). Flexibility and adaptability in binding of E. coli cytidine repressor to different operators suggests a role in differential gene regulation. J Mol Biol 362(2), 271-86.
Weeks, C. S., Tanabe, H., Cummings, J. E., Crampton, S. P., Sheynis, T., Jelinek, R., Vanderlick, T. K., Cocco, M. J., and Ouellette, A. J. (2006). Matrix metalloproteinase-7 activation of mouse paneth cell pro-alpha-defensins: SER43 down arrow ILE44 proteolysis enables membrane-disruptive activity. J Biol Chem 281(39), 28932-42.
Kamtekar, S., Ho, R. S., Cocco, M. J., Li, W., Wenwieser, S. V., Boocock, M. R., Grindley, N. D., and Steitz, T. A. (2006). Implications of structures of synaptic tetramers of gamma delta resolvase for the mechanism of recombination. Proc Natl Acad Sci U S A 103(28), 10642-7.
Levin, A. M., Coroneus, J. G., Cocco, M. J., and Weiss, G. A. (2006). Exploring the interaction between the protein kinase A catalytic subunit and caveolin-1 scaffolding domain with shotgun scanning, oligomer complementation, NMR, and docking. Protein Sci 15(3), 478-86.
Sun, G., Pal, S., Sarcon, A. K., Kim, S., Sugawara, E., Nikaido, H., Cocco, M. J., Peterson, E. M., and de la Maza, L. M. (2007). Structural and functional analyses of the major outer membrane protein of Chlamydia trachomatis. J Bacteriol 189(17), 6222-35. |
