Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus–cell fusion
The C-terminal transmembrane domain (TMD) of viral fusion proteins such as HIV gp41 and influenza hemagglutinin (HA) is traditionally viewed as a passive α-helical anchor of the protein to the virus envelope during its merger with the cell membrane. The conformation, dynamics, and lipid interaction...
Main Authors: | , , , , |
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Other Authors: | |
Format: | Article |
Language: | en_US |
Published: |
National Academy of Sciences (U.S.)
2016
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Online Access: | http://hdl.handle.net/1721.1/101400 https://orcid.org/0000-0001-5255-5858 https://orcid.org/0000-0003-2383-1942 |