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Structural flexibility of the Gαs α-helical domain in the β 2 -adrenoceptor Gs complex

Structural flexibility of the Gαs α-helical domain in the β 2 -adrenoceptor Gs complex

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_citationtrail_10_1073_pnas_1113645108

Structural flexibility of the Gαs α-helical domain in the β 2 -adrenoceptor Gs complex

About this item

Full title

Structural flexibility of the Gαs α-helical domain in the β 2 -adrenoceptor Gs complex

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2011-10, Vol.108 (38), p.16086-16091

Language

English

Formats

More information

Scope and Contents

Contents

The active-state complex between an agonist-bound receptor and a guanine nucleotide-free G protein represents the fundamental signaling assembly for the majority of hormone and neurotransmitter signaling. We applied single-particle electron microscopy (EM) analysis to examine the architecture of agonist-occupied β
2
-adrenoceptor (β
2
A...

Alternative Titles

Full title

Structural flexibility of the Gαs α-helical domain in the β 2 -adrenoceptor Gs complex

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_crossref_citationtrail_10_1073_pnas_1113645108

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_citationtrail_10_1073_pnas_1113645108

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1113645108

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