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Mechanism of intracellular allosteric β 2 AR antagonist revealed by X-ray crystal structure

Mechanism of intracellular allosteric β 2 AR antagonist revealed by X-ray crystal structure

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_28813418

Mechanism of intracellular allosteric β 2 AR antagonist revealed by X-ray crystal structure

About this item

Full title

Mechanism of intracellular allosteric β 2 AR antagonist revealed by X-ray crystal structure

Publisher

England

Journal title

Nature (London), 2017-08, Vol.548 (7668), p.480

Language

English

Formats

Publication information

Publisher

England

More information

Scope and Contents

Contents

G-protein-coupled receptors (GPCRs) pose challenges for drug discovery efforts because of the high degree of structural homology in the orthosteric pocket, particularly for GPCRs within a single subfamily, such as the nine adrenergic receptors. Allosteric ligands may bind to less-conserved regions of these receptors and therefore are more likely to...

Alternative Titles

Full title

Mechanism of intracellular allosteric β 2 AR antagonist revealed by X-ray crystal structure

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmed_primary_28813418

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_28813418

Other Identifiers

E-ISSN

1476-4687

DOI

10.1038/nature23652

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