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
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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Self-citationConformational biosensors reveal GPCR signalling from endosomes
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Structural basis for self-association and receptor recognition of human TRAF2
Park, Y. C., Burkitt, V., Villa, A. R., Tong, L., & Wu, H. (1999) · Nature · doi:10.1038/19110 · Cited by 358
Structural Evidence for a Sequential Release Mechanism for Activation of Heterotrimeric G Proteins
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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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