Faculty: Biography

Cory Momany, Ph.D.
Associate Professor
Pharmaceutical and Biomedical Sciences
Address: R.C. Wilson Pharmacy Building
University of Georgia
Athens, GA 30602
Office: Room 372
Phone: (706) 542-5370
Email: cmomany@mail.rx.uga.edu
Biosketch
Ph.D.University of TexasAustin1990
B.A.Rice UniversityHouston1983
Post-doctoral Experience
Postdoctoral Appointment, Purdue University, West Lafayette, IN, 1992-1996
Honors and Awards
Research Interests
Research is focused on the generation of atomic structures and the application of these atomic structures to pharmaceutical problems. The research program is multidisciplinary in approach and bridges the fields of nanotechnology, molecular biology, biochemistry, pharmacogenomics, and structure-based drug discovery- all centered around the use of macromolecular X-ray crystallography.

Generation of macromolecular structures using novel technologies. New methods of crystallizing macromolecules are being developed using self-assembling matrices coupled with Phage display technology for high-throughput crystallizations. This technology includes using bacterially produced antibody lattices and small proteins with enhanced symmetry features. Ultimately, the technology is targeted for crystallizing pharmacologically important drug metabolism proteins such as Cytochrome p450 monooxygenases and membrane receptor proteins. A current engineering grant, in collaboration with Dr. Bill Dennis in the Physics Department at UGA, is focused on screening for crystals in vivo using non-linear optical methods. The ultimate goal is to apply this technology to the field of nanotechnology as well as to apply the methodologies to the crystallization of macromolecules.

Application of macromolecular structures to pharmaceutical problems. Projects encompass several significantly overlapping research areas. First are collaborative projects focused on drug discovery targeting the human immunodeficiency virus. Considerable purification and crystallization trials have been performed on HIV reverse transcriptase and capsid proteins and are collaborating on several additional HIV proteins. The goal is to obtain diffraction quality crystals of protein-drug complexes and perform structure-based drug design. The second area of research is bacterial regulation of transcriptions. Collaborations with faculty in the Microbiology Department at UGA (Drs. Ellen Neidle, Tim Hoover & Anne Summers) are focused on understanding bacterial transcriptional regulation at a molecular level. The structure determination of a LysR-type transcriptional regulatory effector domain (BenM-EBD) is complete and additional transcriptional regulators have been crystallized or are currently in crystallization trials. The last area of research is focused on structural studies of vitamin B6, pyridoxal-5'-phosphate (PLP) dependent enzymes to understand the biochemical mechanism of the cofactor. Recently the atomic structures of bacterial diaminopimelate decarboxylase and bacterial kynureninase have been solved (collaboration with Robbie Phillips in the Chemistry Department at UGA).
Representative Publications
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.
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