Ph.D. Emory University 1984; B.S. University of West Florida 1980
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NMR-based structural studies indicate that the cellular phosphatidylinosititde, PIP2 (yellow) binds to a conserved cleft on the HIV-1 matrix protein, triggering myristate (green) exposure and membrane binding.
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Our research efforts are aimed at understanding how retroviruses assemble and how they specifically recognized and package their genetic material. Over the past decade or so, we and others have determined the 3D structures of several isolated protein components that make up HIV-1 (the retrovirus that causes AIDS). We now wish to understand how these components interact with each other and with cellular constituents. We are also interested in understanding how these intermolecular interactions change when the initially-formed retrovirus matures and become infectious. In the long term, we would like to use the basic structural and functional information obtained to design new therapeutic approaches for the treatment of AIDS and other human diseases caused by retroviruses.
