Structural and functional studies by our lab and others have confirmed the salient features of this spring-loaded mechanism. The HIV gp41 protein mediates fusion of viral and cellular membranes during the entry process. Thus, our results demonstrate that molecules that bind solely to the pocket can inhibit infection, and they validate the pocket per se as a target for the development of a new class of orally bioavailable drugs that target HIV entry into cells. We are particularly interested in developing ways to elicit a neutralizing antibody response directed against these intermediate states. IQN17 serves as one immunogen to test, especially since the pocket and surrounding structures are conserved among different HIV strains.
Coiled coils are examples of such modules.
We utilize coiled coils as model systems for studying protein folding and protein-protein interactions. A computationally driven experimental approach to analyzing coiled-coil interactions in the yeast genome has begun. A key step was the development of a sidechain-repacking algorithm that allows for backbone motions. Selected Publications Chan, D.C. and Kim, P.S. HIV Entry and Its Inhibition.