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Sci Rep. 2016 Apr 5;6:24029. doi: 10.1038/srep24029.

Combined approaches of EPR and NMR illustrate only one transmembrane helix in the human IFITM3.

Author information

1
Hefei National Laboratory of Microscale Physical Sciences, School of Life Science, University of Science and Technology of China, Hefei, 230027, P. R. China.
2
High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, 230031, P. R. China.

Abstract

Interferon-inducible transmembrane protein IFITM3 was known to restrict the entry of a wide spectrum of viruses to the cytosol of the host. The mechanism used by the protein to restrict viral entry is unclear given the unavailability of the membrane topology and structures of the IFITM family proteins. Systematic site-directed spin labeling (SDSL) and electron paramagnetic resonance (EPR) studies of IFITM3 in detergent micelles identified a single, long transmembrane helix in the C-terminus and an intramembrane segment in the N-terminal hydrophobic region. Solution NMR studies of the same sample verified the secondary structure distribution and demonstrated two rigid regions interacting with the micellar surface. The resulting membrane topology of IFITM3 supports the mechanism of an enhanced restricted membrane hemi-fusion.

PMID:
27046158
PMCID:
PMC4820770
DOI:
10.1038/srep24029
[Indexed for MEDLINE]
Free PMC Article

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