BIOL 153 |
| Understanding the nature of helix-helix interactions in the putative three-helix bundle formation of the gp41 transmembrane (TM) domain is essential for control of virus-cell membrane fusion in HIV-1 infection. Molecular dynamics was used to analyze and compare the conformations of the right- and left-handed three-helix bundles in a hydrated palmitoyl-oleoyl-phosphatidylethanolamine (POPE) lipid bilayer over the course of several 18-ns simulations. While the three-helix bundles showed instability in DMSO, decane, and water, the integrity of the helix bundles and the helical structure appeared to remain intact in the hydrated lipid bilayer for the duration of each of the 18-ns simulations, based on analysis of inter-strand hydrogen bonds, Cα RMSD, and helical properties. These observations suggest that formation of the three-helix bundle of the TM domain, whether right- or left-handed, may be essential in trimeric formation of gp41, thought to occur during the virus-cell membrane fusion process. |
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Chemistry and Metabolism
4:30 PM-6:30 PM, Tuesday, 12 September 2006 Moscone Center -- Hall D, Poster
Division of Biological Chemistry |