Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trime...
Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly
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Author / Creator
Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS) , Xu, Kai , Chan, Yee-Peng , Bradel-Tretheway, Birgit , Akyol-Ataman, Zeynep , Zhu, Yongqun , Dutta, Somnath , Yan, Lianying , Feng, YanRu , Wang, Lin-Fa , Skiniotis, Georgios , Lee, Benhur , Zhou, Z. Hong , Broder, Christopher C. , Aguilar, Hector C. and Nikolov, Dimitar B.
Publisher
United States: Public Library of Science
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Language
English
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United States: Public Library of Science
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Scope and Contents
Contents
Nipah virus (NiV) is a paramyxovirus that infects host cells through the coordinated efforts of two envelope glycoproteins. The G glycoprotein attaches to cell receptors, triggering the fusion (F) glycoprotein to execute membrane fusion. Here we report the first crystal structure of the pre-fusion form of the NiV-F glycoprotein ectodomain. Interest...
Alternative Titles
Full title
Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly
Authors, Artists and Contributors
Author / Creator
Xu, Kai
Chan, Yee-Peng
Bradel-Tretheway, Birgit
Akyol-Ataman, Zeynep
Zhu, Yongqun
Dutta, Somnath
Yan, Lianying
Feng, YanRu
Wang, Lin-Fa
Skiniotis, Georgios
Lee, Benhur
Zhou, Z. Hong
Broder, Christopher C.
Aguilar, Hector C.
Nikolov, Dimitar B.
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Primary Identifiers
Record Identifier
TN_cdi_plos_journals_1773863002
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1773863002
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ISSN
1553-7374,1553-7366
E-ISSN
1553-7374
DOI
10.1371/journal.ppat.1005322