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Conformational states of the full-length glucagon receptor

Conformational states of the full-length glucagon receptor

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4532856

Conformational states of the full-length glucagon receptor

About this item

Full title

Conformational states of the full-length glucagon receptor

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2015-07, Vol.6 (1), p.7859-7859, Article 7859

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Class B G protein-coupled receptors are composed of an extracellular domain (ECD) and a seven-transmembrane (7TM) domain, and their signalling is regulated by peptide hormones. Using a hybrid structural biology approach together with the ECD and 7TM domain crystal structures of the glucagon receptor (GCGR), we examine the relationship between full-...

Alternative Titles

Full title

Conformational states of the full-length glucagon receptor

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4532856

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4532856

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms8859

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