My lab uses X-ray crystallography to better understand the relationship between proteins and ligands. Tiny differences in the structure of a molecule can radically change the interaction between a protein and ligand and we are only begining to understand how many factors play a role in this interaction. By manipulating the individual components of a compound it is possible to create a chemical that binds to the protein better than the natural substrate, and prevent the natural reaction from occurring. This is the basis for rational drug design. Our efforts have lead us to collaborations with other labs and scientists in many disciplines as our approach to directed compound design has applications not only in basic research but also in pesticide development, health research and clinical research.
- O'Hagan, R. C., Schreiber-Agus, N., Chen, K., David, G., Engelman, J. A., Schwab, R., ... DePinho, R. A. (2000). Gene-target recognition among members of the Myc superfamily and implications for oncogenesis. NATURE GENETICS. 24(2), 113-119.
- Eicken, C., Krebs, B., & Sacchettini, J. C. (1999). Catechol oxidase - structure and activity. CURRENT OPINION IN STRUCTURAL BIOLOGY. 9(6), 677-683.
- Rozwarski, D. A., Vilcheze, C., Sugantino, M., Bittman, R., & Sacchettini, J. C. (1999). Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate. International Journal of Leprosy and Other Mycobacterial Diseases. 67(4 SUPPL.), 517.
- Balendiran, G. K., Molina, J. A., Xu, Y., Torres-Martinez, J., Stevens, R., Focia, P. J., ... Craig, S. P. (1999). Erratum: Ternary complex structure of human HGPRTase, PRPP, Mg2+, and the inhibitor HPP reveals the involvement of the flexible loop in substrate binding (Protein Science (1999) 8:5 (1023-1031)). Protein Sci. 8(12), 2815.
- Balendiran, G. K., Molina, J. A., Xu, Y. M., Torres-Martinez, J., Stevens, R., Focia, P. J., ... Craig, S. P. (1999). Ternary complex structure of human HGPRTase, PRPP, Mg2+, and the inhibitor HPP reveals the involvement of the flexible loop in substrate binding (vol 8, pg 1023, 1999). Protein Sci. 8(12), 2815-2815.
- Musa, T. L., Ioerger, T. R., & Sacchettini, J. C. (2009). THE TUBERCULOSIS STRUCTURAL GENOMICS CONSORTIUM: A STRUCTURAL GENOMICS APPROACH TO DRUG DISCOVERY. Advances in protein chemistry and structural biology. STRUCTURAL GENOMICS, PART C. (pp. 41-76).
- Reddy, M., Sacchettini, J. C., Zhou, N. E., & Mccutchen, B. F. (2019). Compositions and methods for inhibition of mycobacteria.
- Sacchettini, J. C., Miller, M. W., Wallis, D., Zhou, N. E., & Fossum, T. W. (2019). Compositions and methods for drug sensitization of parasites.
- Sacchettini, J., Zhou, N., Baker, D., Maxwell, S., & Wallis, D. (2018). Compositions and methods for drug-sensitization or inhibition of a cancer cell.
- Rao, J., Cirillo, J., Xie, H., & Sacchettini, J. (2017). ?-lactamase substrates and methods of their use for the diagnosis of tuberculosis.
- Rao, J., Cirillo, J. D., Xie, H., & Sacchettini, J. C. (2017). β-lactamase substrates and methods of their use for the diagnosis of tuberculosis.
- Harshbarger, Wayne (2015-05). X-Ray Crystal Structure of Human 20s Proteasome in Complex with Carfilzomib. (Doctoral Dissertation)
- Jung, Hunmin (2014-12). Development of Potent and Selective Inhibitors of Mycobacterium Tuberculosis, Plasmodium Falciparum and Staphylococcus Aureus Dihydrofolate Reductase. (Doctoral Dissertation)
- Joseph, Sonia (2014-08). The Biochemical Investigation and Isolation of Small Molecule Inhibitors for Two Essential Proteins of Mycobacterium tuberculosis H37Rv: IspD and Wag31. (Master's Thesis)
- Lalgondar, Mallikarjun (2014-05). Structural Studies and Evaluation of Inhibitors of Mycobacterium tuberculosis H37Rv Shikimate Dehydrogenase (MtSDH). (Master's Thesis)