I study the structural basis of dimerization and maturation of HIV-1 reverse transcriptase (RT). This viral enzyme is a primary target in the current treatments for HIV-1 infection. The biologically active form of the enzyme requires dimerization of the RT subunits and proteolytic processing of one of these subunits. Little structural data currently exists regarding the mechanisms of these dimerization and maturation processes which could provide attractive therapeutic targets for future antiretroviral therapies. Our lab uses solution nuclear magnetic resonance (NMR) spectroscopy to determine structures of viral enzymes, and integrate our structural understanding into further mechanistic and functional studies.
B. Sc. in Biophysics, Centenary College of Louisiana, 2006
PhD Advisor: Dr. Rieko Ishima
Biomedical Science Tower 3
3501 Fifth Ave.
Pittsburgh, PA 15260
- Cornelius J, Tran T, Turner N, Piazza A, Mills L, Slack R, Hauser S, Alexander JS, Grisham MB, Feelisch M, Rodriguez J. “Isotope tracing enhancement of chemiluminescence assays for nitric oxide research” Biol Chem. Feb;390(2):181-9 (2009)
- Sharaf NG, Poliner E, Slack RL, Christen MT, Byeon IJ, Parniak MA, Gronenborn AM, Ishima R. The p66 immature precursor of HIV-1 reverse transcriptase. Proteins. 2014; 82(10):2343-52
- Slack RL, Spiriti J, Ahn J, Parniak MA, Zuckerman DM, Ishima R. (2015) Structural integrity of the ribonuclease H domain in HIV-1 reverse transcriptase. Proteins. 83(8):1526-38
- Karki I, Christen MT, Spiriti J, Slack RL, Oda M, Kanaori K, Zuckerman DM, Ishima R. Entire-Dataset Analysis of NMR Fast-Exchange Titration Spectra: A Mg2+ Titration Analysis for HIV-1 Ribonuclease H Domain. J Phys Chem B. 2016; 120(49):12420-12431.