Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)
- 2003.06a
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- Pages.58-58
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- 2003
Membrane interaction of the coiled-coil motif of HIV gp41 and its implication in the membrane fusion process
- Jin, Bong-Suk (Division of Life Sciences, Korea Institute of Science and Technology) ;
- Yu, Yeon-Gyu (Division of Life Sciences, Korea Institute of Science and Technology)
- Published : 2003.06.01
Abstract
The envelope glycoprotein of HIV, gp41, mediates the membrane fusion with human cells. The extracellular domain of gp41 has two helical regions. The N-terminus helical region (N-helix) forms trimeric coiled coil, interacts with the C-terminus helical region (C-helix) of gp41 to form a stable helical bundle structure. In this study, we have shown that the N-helix of gp41 has membrane interacting and disrupting abilities. It was localized into the interface of the lipidic phase and head group of the membrane. In contrast, the N-helix region with membrane fusion defective mutations could not bind to membrane. In addition, the N-helix bound on the membrane was released from the membrane by the C-helix, and the complex of the N- and C-helix did not interact with membrane. These results suggested that the membrane binding ability of the N-helix is necessary for the fusion activity of gp41, and such property is possibly controlled by the C-helm.
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