The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
Open accessAbstract
Enveloped viruses have evolved complex glycoprotein machinery that drives the fusion of viral and cellular membranes, permitting entry of the viral genome into the cell. For the paramyxoviruses, the fusion (F) protein catalyses this membrane merger and entry step, and it has been postulated that the F protein undergoes complex refolding during this process. Here we report the crystal structure of the parainfluenza virus 5 F protein in its prefusion conformation, stabilized by the addition of a carboxy-terminal trimerization domain. The structure of the F protein shows that there are profound conformational differences between the pre- and postfusion states, involving transformations in secondary and tertiary structure. The positions and structural transitions of key parts of the fusion machinery, including the hydrophobic fusion peptide and two helical heptad repeat regions, clarify the mechanism of membrane fusion mediated by the F protein.
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Cites
Structure of influenza haemagglutinin at the pH of membrane fusion
Bullough, P. A., Hughson, F. M., Skehel, J. J., & Wiley, D. C. (1994) · Nature · doi:10.1038/371037a0 · Cited by 1,564
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490 · cited 2×
“A soluble form of F was generated that contained the honeybee melittin signal sequence in place of the F signal sequence and, at the C terminus, an isoleucine zipper domain (GCNt) 23,42 in heptad repeat phase with HRB, followed by a factor Xa cleavage site and a His 6 tag.”
Crystal structure of an isoleucine-zipper trimer
Harbury, P. B., Kim, P. S., & Alber, T. (1994) · Nature · doi:10.1038/371080a0 · Cited by 472
Cited by
Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme
White, J. M., Delos, S. E., Brecher, M., & Schornberg, K. (2008) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230802058320 · Cited by 892
Structure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody
McLellan, J. S., Chen, M., Leung, S., Graepel, K. W., Du, X., Yang, Y., Zhou, T., Baxa, U., Yasuda, E., Beaumont, T., et al. (2013) · Science · doi:10.1126/science.1234914 · Cited by 883
Structural insights into coronavirus entry
(2019) · Advances in Virus Research · doi:10.1016/bs.aivir.2019.08.002 · Cited by 769
Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer
Walls, A. C., Tortorici, M. A., Bosch, B.-J., Frenz, B., Rottier, P. J. M., DiMaio, F., Rey, F. A., & Veesler, D. (2016) · Nature · doi:10.1038/nature16988 · Cited by 538
Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion
Walls, A. C., Tortorici, M. A., Snijder, J., Xiong, X., Bosch, B.-J., Rey, F. A., & Veesler, D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708727114 · Cited by 537
Metadata
- Authors
- Yin, H.-S., Wen, X., Paterson, R. G., Lamb, R. A., & Jardetzky, T. S.
- Venue
- Nature
- Published
- 2006-01-05
- Volume
- 439
- Issue
- 7072
- Pages
- 38-44
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1972940026
- Cited by
- 418
- References
- 3
- FWCI
- 21.03
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Yin, H.-S., Wen, X., Paterson, R. G., Lamb, R. A., & Jardetzky, T. S. (2006). Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature. https://doi.org/10.1038/nature04322
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