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6N48

Structure of beta2 adrenergic receptor bound to BI167107, Nanobody 6B9, and a positive allosteric modulator

Summary for 6N48
Entry DOI10.2210/pdb6n48/pdb
DescriptorEndolysin,Beta-2 adrenergic receptor,Beta-2 adrenergic receptor chimera, Camelid Antibody Fragment, 8-[(1R)-2-{[1,1-dimethyl-2-(2-methylphenyl)ethyl]amino}-1-hydroxyethyl]-5-hydroxy-2H-1,4-benzoxazin-3(4H)-one, ... (5 entities in total)
Functional Keywordsg protein coupled receptor, membrane protein, signaling protein
Biological sourceEnterobacteria phage RB59
More
Total number of polymer chains2
Total formula weight67761.14
Authors
Liu, X.,Masoudi, A.,Kahsai, A.W.,Huang, L.Y.,Pani, B.,Hirata, K.,Ahn, S.,Lefkowitz, R.J.,Kobilka, B.K. (deposition date: 2018-11-17, release date: 2019-06-26, Last modification date: 2024-11-06)
Primary citationLiu, X.,Masoudi, A.,Kahsai, A.W.,Huang, L.Y.,Pani, B.,Staus, D.P.,Shim, P.J.,Hirata, K.,Simhal, R.K.,Schwalb, A.M.,Rambarat, P.K.,Ahn, S.,Lefkowitz, R.J.,Kobilka, B.
Mechanism of beta2AR regulation by an intracellular positive allosteric modulator.
Science, 364:1283-1287, 2019
Cited by
PubMed Abstract: Drugs targeting the orthosteric, primary binding site of G protein-coupled receptors are the most common therapeutics. Allosteric binding sites, elsewhere on the receptors, are less well-defined, and so less exploited clinically. We report the crystal structure of the prototypic β-adrenergic receptor in complex with an orthosteric agonist and compound-6FA, a positive allosteric modulator of this receptor. It binds on the receptor's inner surface in a pocket created by intracellular loop 2 and transmembrane segments 3 and 4, stabilizing the loop in an α-helical conformation required to engage the G protein. Structural comparison explains the selectivity of the compound for β- over the β-adrenergic receptor. Diversity in location, mechanism, and selectivity of allosteric ligands provides potential to expand the range of receptor drugs.
PubMed: 31249059
DOI: 10.1126/science.aaw8981
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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