The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
Crystal structure of oligomeric β1-adrenergic G protein–coupled receptors in ligand-free basal state
Open accessAbstract
G protein–coupled receptors (GPCRs) mediate transmembrane signaling. Before ligand binding, GPCRs exist in a basal state. Crystal structures of several GPCRs bound with antagonists or agonists have been solved. However, the crystal structure of the ligand-free basal state of a GPCR, the starting point of GPCR activation and function, had not yet been determined. Here we report the X-ray crystal structure of the ligand-free basal state of a GPCR in a lipid membrane–like environment. Oligomeric turkey β1-adrenergic receptors display two dimer interfaces. One interface involves the transmembrane domain (TM) 1, TM2, the C-terminal H8 and extracellular loop 1. The other interface engages residues from TM4, TM5, intracellular loop 2 and extracellular loop 2. Structural comparisons show that this ligand-free state is in an inactive conformation. This provides the structural basis of GPCR dimerization and oligomerization.
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Metadata
- Authors
- Huang, J., Chen, S., Zhang, J. J., & Huang, X.-Y.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2013-02-24
- Volume
- 20
- Issue
- 4
- Pages
- 419-425
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2017713787
- Cited by
- 261
- References
- 63
- FWCI
- 15.87
- Type
- journal article
- Language
- en
- Open access
- green
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