Ph.D., University of Texas 1990
B.A. Biochemistry, Rice University 1983
Dr. Momany’s research is focused on the application of atomic structures to biological and pharmaceutical problems. The research program is multidisciplinary in approach and bridges the fields of molecular biology, biochemistry, and structure-based drug discovery- all centered around the use of macromolecular X-ray crystallography.
Current funded research is focused on understanding the process of bacterial transcriptional activation at a structural level. Two families of transcriptional regulators are being studied, the MerR and LysR-type transcriptional regulator family, as model systems. LTTRs are the largest family of regulators in bacteria, and as such display a wide range of functions spanning nitrogen fixation to virulence. Our studies have far-reaching applications in the areas of bioremediation and drug discovery.
One ongoing project in the laboratory is the development of new means to produce antibodies for use as new therapeutics and crystallization vehicles. Large-scale production of antibody therapeutics is possible in bacterial expression systems. Using powerful in vitro selection systems, new antibodies can be obtained rapidly without using mouse hybridoma technology. Cocrystallization of proteins with antibodies is a powerful method for crystallizing membrane-associate proteins that are otherwise extremely difficult to study. Another project is focused on the drug discovery for Alzheimer’s disease targeting the kynurenine pathway (tryptophan metabolism). Using a structure-guided approach, we are designing inhibitors of the pathway that can increase neuroprotective molecules while reducing neurotoxic intermediates.
- National Science Foundation
- Department of Energy, Office of Science
Alanazi Am, Neidle El, Momany C. (2013) “The Dna-Binding Domain Of BenM Reveals The Structural Basis For The Recognition Of A T-N11-A Sequence Motif By LysR-Type Transcriptional Regulators.” Acta Crystallogr D Biol Crystallogr. 2013 Oct; 69(Pt 10):1995-2007. DOI 10.1107/S0907444913017320. Epub 2013 Sep 20.
Nickolaus R. Galloway, Hannah Toutkoushian, Melesse Nune, Nandita Bose, and Momany C. (2013) “Rapid Cloning For Protein Crystallography Using Type IIs Restriction Enzymes”, Cryst. Growth Des, 13 (7), pp 2833–2839, DOI: 10.1021/Cg400171z, May 16, 2013 (Web)
Momany C, Neidle EL. “Defying stereotypes: the elusive search for a universal model of LysR-type regulation.” Mol Microbiol. Feb;83(3):453-6. doi: 10.1111/j.1365-2958.2011.07960.x [Epub 2012 Jan 11], 2012.
Ruangprasert A., Craven S.H., Neidle E.L., and Momany C. (2010) “Full-Length Structures of BenM and Two Variants Reveal Different Oligomerization Schemes For LysR-Type Transcriptional Regulators” J. Mol. Biol. 404:568–586.
Parks J.M., Guo H., Momany C., Liang L., Miller S.M., Summers A.O., and Smith J.C. (2009) “Mechanism of Hg-C protonolysis in the organomercurial lyase MerB.” J Am Chem Soc. 131(37):13278-85.
Craven S.H., Ezezika O.C., Haddad S., Hall R.A., Momany C., and Neidle E.L. (2009) “Inducer responses of BenM, a LysR-type transcriptional regulator from Acinetobacter baylyi ADP1.” Mol Microbiol. 72(4):881-94. Epub 2009 Apr 8.
Lima S., Sundararaju B., Huang C., Khristoforov R., Momany C., and Phillips R.S. (2009) “The crystal structure of the Pseudomonas dacunhae aspartate-beta-decarboxylase dodecamer reveals an unknown oligomeric assembly for a pyridoxal-5′-phosphate-dependent enzyme.” J Mol Biol. 2009 Apr 24;388(1):98-108. Epub 2009 Mar 2.
Lima S., Kumar S., Gawandi V., Momany C., and Phillips R.S. (2009) “Crystal structure of the Homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex: insights into the molecular basis of kynureninase substrate specificity.” J Med Chem. 52(2):389-96.