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A conserved TLR5 binding and activation hot spot on flagellin

A conserved TLR5 binding and activation hot spot on flagellin

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5247705

A conserved TLR5 binding and activation hot spot on flagellin

About this item

Full title

A conserved TLR5 binding and activation hot spot on flagellin

Publisher

London: Nature Publishing Group UK

Journal title

Scientific reports, 2017-01, Vol.7 (1), p.40878-40878, Article 40878

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Flagellin is a bacterial protein that polymerizes into the flagellar filament and is essential for bacterial motility. When flagellated bacteria invade the host, flagellin is recognized by Toll-like receptor 5 (TLR5) as a pathogen invasion signal and eventually evokes the innate immune response. Here, we provide a conserved structural mechanism by...

Alternative Titles

Full title

A conserved TLR5 binding and activation hot spot on flagellin

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5247705

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5247705

Other Identifiers

ISSN

2045-2322

E-ISSN

2045-2322

DOI

10.1038/srep40878

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