Crystal Structure of the β2Adrenergic Receptor-Gs protein complex
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Summary
This crystal structure represents the first high-resolution view of transmembrane signalling by a GPCR and the most surprising observation is a major displacement of the α-helical domain of Gαs relative to the Ras-like GTPase domain.
- Type
- article
- Published
- 2011-07-19
- Cited by
- 2,935
- References
- 61
- Access
- Open access
- OpenAlex
- https://openalex.org/W2167857702
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:3452645
Keywords
Adrenergic receptor, Crystal structure, Receptor, Adrenergic, Chemistry
References
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- Amino and carboxyl terminal modifications to facilitate the production and purification of a G protein-coupled receptor.
- Separate GTP binding and GTPase activating domains of a G alpha subunit.
- Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis.
- Membrane protein crystallization in lipidic mesophases with tailored bilayers.
- Super-resolution biomolecular crystallography with low-resolution data
- Structure of a nanobody-stabilized active state of the β2 adrenoceptor
- Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit
- A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
- Heterotrimeric G protein activation by G-protein-coupled receptors
- The mammalian beta 2-adrenergic receptor: reconstitution of functional interactions between pure receptor and pure stimulatory nucleotide binding protein of the adenylate cyclase system.
- Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin
- Structure-based analysis of GPCR function: evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein.
- β2 adrenergic receptor-induced conformational changes in the heterotrimeric G protein Gs
Cited by
- Arrestin interactions with G protein-coupled receptors.
- Crystallizing membrane proteins for structure–function studies using lipidic mesophases
- Structural dynamics of transmembrane signaling complexes by negative stain electron microscopy
- Tools for GPCR drug discovery
- Functional fusions of T4 lysozyme in the third intracellular loop of a G protein-coupled receptor identified by a random screening approach in yeast.
- GPCR activation: a mutagenic spotlight on crystal structures.
- Beyond Standard Molecular Dynamics: Investigating the Molecular Mechanisms of G Protein-Coupled Receptors with Enhanced Molecular Dynamics Methods
- An automated approach to network features of protein structure ensembles
- Strike a Pose: Gαq Complexes at the Membrane
- Constitutive activity in gonadotropin receptors.
- Active-State Model of a Dopamine D2 Receptor - Gαi Complex Stabilized by Aripiprazole-Type Partial Agonists
- Structural features of β2 adrenergic receptor: crystal structures and beyond.
- 2D Projection Analysis of GPCR Complexes by Negative Stain Electron Microscopy.
- A high-transparency, micro-patternable chip for X-ray diffraction analysis of microcrystals under native growth conditions
- Functional reversal of (−)‐Stepholidine analogues by replacement of benzazepine substructure using the ring‐expansion strategy
- Towards understanding the structural basis of partial agonism at the dopamine D3 receptor
- HTS-compatible FRET-based conformational sensors clarify membrane receptor activation.
- Structural and Functional Analysis of a β2-Adrenergic Receptor Complex with GRK5
- Structural mechanism of arrestin activation.
- Structure-inspired design of β-arrestin-biased ligands for aminergic GPCRs
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