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Cited by 320

The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.

Crystal Structure of the Adenylyl Cyclase Activator G s α

Sunahara, Roger K., Tesmer, John J. G., Gilman, Alfred G., Sprang, Stephen R.·1997·Science

Abstract

The crystal structure of G s α , the heterotrimeric G protein α subunit that stimulates adenylyl cyclase, was determined at 2.5 Å in a complex with guanosine 5′- O -(3-thiotriphosphate) (GTPγS). G s α is the prototypic member of a family of GTP-binding proteins that regulate the activities of effectors in a hormone-dependent manner. Comparison of the structure of G s α ·GTPγS with that of G i α ·GTPγS suggests that their effector specificity is primarily dictated by the shape of the binding surface formed by the switch II helix and the α3-β5 loop, despite the high sequence homology of these elements. In contrast, sequence divergence explains the inability of regulators of G protein signaling to stimulate the GTPase activity of G s α . The βγ binding surface of G s α is largely conserved in sequence and structure to that of G i α , whereas differences in the surface formed by the carboxyl-terminal helix and the α4-β6 loop may mediate receptor specificity.

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Metadata

Authors
Sunahara, R. K., Tesmer, J. J. G., Gilman, A. G., & Sprang, S. R.
Venue
Science
Published
1997-12-12
Volume
278
Issue
5345
Pages
1943-1947
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2093626313
Cited by
320
References
33
FWCI
5.96
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Crystal Structure of the Adenylyl Cyclase Activator G s α. https://app.cochat.ai/papers/10.1126/science.278.5345.1943
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Sunahara, R. K., Tesmer, J. J. G., Gilman, A. G., & Sprang, S. R. (1997). Crystal Structure of the Adenylyl Cyclase Activator G s α. Science. https://doi.org/10.1126/science.278.5345.1943

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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