期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1768, 期 12, 页码 3052-3060出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2007.09.010
关键词
solution spectroscopy; EPR spectroscopy; membrane fusion domain; influenza virus; human immunodeficiency virus
资金
- NIAID NIH HHS [R01 AI030557-11, R37 AI030557, R01 AI030557] Funding Source: Medline
- NIGMS NIH HHS [P01 GM072694-03, P01 GM072694] Funding Source: Medline
Methods are described to determine the structures of viral membrane fusion domains in detergent micelles by NMR and in lipid bilayers by site-directed spin labeling and EPR spectroscopy. Since in favorable cases, the lower-resolution spin label data obtained in lipid bilayers fully support the higher-resolution structures obtained by solution NMR, it is possible to graft the NMR structural coordinates into membranes using the EPR-derived distance restraints to the lipid bilayer. Electron paramagnetic dynamics and distance measurements in bilayers support conclusions drawn from NMR in detergent micelles. When these methods are applied to a structure determination of the influenza virus fusion domain and four point mutations with different functional phenotypes, it is evident that a fixed-angle boomerang structure with a glycine edge on the outside of the N-terminal arm is both necessary and sufficient to support membrane fusion. The human immunodeficiency virus fusion domain forms a straight helix with a flexible C-terminus. While EPR data for this fusion domain are not yet available, it is tentatively speculated that, because of its higher hydrophobicity, a critically tilted insertion may occur even in the absence of a kinked boomerang structure in this case. (C) 2007 Elsevier B.V. All rights reserved.
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