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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-Trime...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1773863002

Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly

About this item

Full title

Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly

Publisher

United States: Public Library of Science

Journal title

PLoS pathogens, 2015-12, Vol.11 (12), p.e1005322

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

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

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1773863002

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1773863002

Other Identifiers

ISSN

1553-7374,1553-7366

E-ISSN

1553-7374

DOI

10.1371/journal.ppat.1005322

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