Combined approaches of EPR and NMR illustrate only one transmembrane helix in the human IFITM3
Identifieur interne : 000873 ( Main/Curation ); précédent : 000872; suivant : 000874Combined approaches of EPR and NMR illustrate only one transmembrane helix in the human IFITM3
Auteurs : Shenglong Ling [République populaire de Chine] ; Chengwei Zhang [République populaire de Chine] ; Wei Wang [République populaire de Chine] ; Xiaoying Cai [République populaire de Chine] ; Lu Yu [République populaire de Chine] ; Fangming Wu [République populaire de Chine] ; Longhua Zhang [République populaire de Chine] ; Changlin Tian [République populaire de Chine]Source :
- Scientific Reports [ 2045-2322 ] ; 2016.
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.
Url:
DOI: 10.1038/srep24029
PubMed: 27046158
PubMed Central: 4820770
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PMC:4820770Le document en format XML
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<front><div type="abstract" xml:lang="en"><p>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.</p>
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