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Structural basis for sulfation-dependent self-glycan recognition by the human immune-inhibitory rece...

Structural basis for sulfation-dependent self-glycan recognition by the human immune-inhibitory rece...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4961179

Structural basis for sulfation-dependent self-glycan recognition by the human immune-inhibitory receptor Siglec-8

About this item

Full title

Structural basis for sulfation-dependent self-glycan recognition by the human immune-inhibitory receptor Siglec-8

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2016-07, Vol.113 (29), p.E4170-E4179

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Siglec-8 is a human immune-inhibitory receptor that, when engaged by specific self-glycans, triggers eosinophil apoptosis and inhibits mast cell degranulation, providing an endogenous mechanism to down-regulate immune responses of these central inflammatory effector cells. Here we used solution NMR spectroscopy to dissect the fine specificity of Si...

Alternative Titles

Full title

Structural basis for sulfation-dependent self-glycan recognition by the human immune-inhibitory receptor Siglec-8

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4961179

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4961179

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1602214113

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