The membrane proximal region (MPR, residues 649–683) and transmembrane domain (TMD, residues 684–705) of the gp41 subunit of HIV-1’s envelope protein are highly conserved and are important in viral mucosal transmission, virus attachment and membrane fusion with target cells.
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- Gong, Zhen (Author)
- Martin Garcia, Jose Manuel (Author)
- Daskalova, Sasha (Author)
- Craciunescu, Felicia (Author)
- Song, Lusheng (Author)
- Dorner, Katerina (Author)
- Hansen, Debra (Author)
- Yang, Jay-How (Author)
- LaBaer, Joshua (Author)
- Hogue, Brenda (Author)
- Mor, Tsafrir (Author)
- Fromme, Petra (Author)
- Department of Chemistry and Biochemistry (Contributor)
- Biodesign Institute (Contributor)
- Applied Structural Discovery (Contributor)
- Infectious Diseases and Vaccinology (Contributor)
- Innovations in Medicine (Contributor)
- Personalized Diagnostics (Contributor)
- College of Liberal Arts and Sciences (Contributor)
- School of Life Sciences (Contributor)
- Digital object identifier: 10.1371/journal.pone.0136507
- Identifier TypeInternational standard serial numberIdentifier Value1045-3830
- Identifier TypeInternational standard serial numberIdentifier Value1939-1560
- The article is published at http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0136507, opens in a new window
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Gong, Z., Martin-Garcia, J. M., Daskalova, S. M., Craciunescu, F. M., Song, L., Dörner, K., . . . Fromme, P. (2015). Biophysical Characterization of a Vaccine Candidate against HIV-1: The Transmembrane and Membrane Proximal Domains of HIV-1 gp41 as a Maltose Binding Protein Fusion. Plos One, 10(8). doi:10.1371/journal.pone.0136507