Combined approaches of EPR and NMR illustrate only one transmembrane helix in the human IFITM3
Identifieur interne : 000328 ( Pmc/Curation ); précédent : 000327; suivant : 000329Combined 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.
The online version of this article (doi:10.1038/srep24029) contains supplementary material, which is available to authorized users.
Url:
DOI: 10.1038/srep24029
PubMed: 27046158
PubMed Central: 4820770
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<front><div type="abstract" xml:lang="en"><p id="Par1">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>
<sec><title>Supplementary information</title>
<p>The online version of this article (doi:10.1038/srep24029) contains supplementary material, which is available to authorized users.</p>
</sec>
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<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Sci Rep</journal-id>
<journal-id journal-id-type="iso-abbrev">Sci Rep</journal-id>
<journal-title-group><journal-title>Scientific Reports</journal-title>
</journal-title-group>
<issn pub-type="epub">2045-2322</issn>
<publisher><publisher-name>Nature Publishing Group UK</publisher-name>
<publisher-loc>London</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">27046158</article-id>
<article-id pub-id-type="pmc">4820770</article-id>
<article-id pub-id-type="publisher-id">BFsrep24029</article-id>
<article-id pub-id-type="doi">10.1038/srep24029</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Combined approaches of EPR and NMR illustrate only one transmembrane helix in the human IFITM3</article-title>
</title-group>
<contrib-group><contrib contrib-type="author" equal-contrib="yes"><name><surname>Ling</surname>
<given-names>Shenglong</given-names>
</name>
<xref ref-type="aff" rid="Aff1">1</xref>
</contrib>
<contrib contrib-type="author" equal-contrib="yes"><name><surname>Zhang</surname>
<given-names>Chengwei</given-names>
</name>
<xref ref-type="aff" rid="Aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wang</surname>
<given-names>Wei</given-names>
</name>
<xref ref-type="aff" rid="Aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Cai</surname>
<given-names>Xiaoying</given-names>
</name>
<xref ref-type="aff" rid="Aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Yu</surname>
<given-names>Lu</given-names>
</name>
<xref ref-type="aff" rid="Aff2">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wu</surname>
<given-names>Fangming</given-names>
</name>
<xref ref-type="aff" rid="Aff2">2</xref>
</contrib>
<contrib contrib-type="author" corresp="yes"><name><surname>Zhang</surname>
<given-names>Longhua</given-names>
</name>
<address><email>zlhustc@ustc.edu.cn</email>
</address>
<xref ref-type="aff" rid="Aff1">1</xref>
</contrib>
<contrib contrib-type="author" corresp="yes"><name><surname>Tian</surname>
<given-names>Changlin</given-names>
</name>
<address><email>cltian@ustc.edu.cn</email>
</address>
<xref ref-type="aff" rid="Aff1">1</xref>
<xref ref-type="aff" rid="Aff2">2</xref>
</contrib>
<aff id="Aff1"><label>1</label>
<institution-wrap><institution-id institution-id-type="GRID">grid.59053.3a</institution-id>
<institution-id institution-id-type="ISNI">0000000121679639</institution-id>
<institution>Hefei National Laboratory of Microscale Physical Sciences, School of Life Science, University of Science and Technology of China,</institution>
</institution-wrap>
Hefei, 230027 P. R. China</aff>
<aff id="Aff2"><label>2</label>
<institution-wrap><institution-id institution-id-type="GRID">grid.467854.c</institution-id>
<institution-id institution-id-type="ISNI">0000 0004 5902 1885</institution-id>
<institution>High Magnetic Field Laboratory, Chinese Academy of Sciences,</institution>
</institution-wrap>
Hefei, 230031 P. R. China</aff>
</contrib-group>
<pub-date pub-type="epub"><day>5</day>
<month>4</month>
<year>2016</year>
</pub-date>
<pub-date pub-type="pmc-release"><day>5</day>
<month>4</month>
<year>2016</year>
</pub-date>
<pub-date pub-type="collection"><year>2016</year>
</pub-date>
<volume>6</volume>
<elocation-id>24029</elocation-id>
<history><date date-type="received"><day>17</day>
<month>12</month>
<year>2015</year>
</date>
<date date-type="accepted"><day>18</day>
<month>3</month>
<year>2016</year>
</date>
</history>
<permissions><copyright-statement>© The Author(s) 2016</copyright-statement>
<license license-type="OpenAccess"><license-p>This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit <ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</ext-link>
</license-p>
</license>
</permissions>
<abstract id="Abs1"><p id="Par1">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>
<sec><title>Supplementary information</title>
<p>The online version of this article (doi:10.1038/srep24029) contains supplementary material, which is available to authorized users.</p>
</sec>
</abstract>
<kwd-group kwd-group-type="npg-subject"><title>Subject terms</title>
<kwd>Biophysics</kwd>
<kwd>Structural biology</kwd>
</kwd-group>
<custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name>
<meta-value>© The Author(s) 2016</meta-value>
</custom-meta>
</custom-meta-group>
</article-meta>
</front>
</pmc>
</record>
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