6h7j

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ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND AGONIST ISOPRENALINE AND NANOBODY Nb80

Structural highlights

6h7j is a 6 chain structure with sequence from Escherichia coli K-12, Lama glama and Meleagris gallopavo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:2CV, 5FW, NA
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THIO_ECOLI Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.

Publication Abstract from PubMed

G protein-coupled receptors (GPCRs) in the G protein-coupled active state have higher affinity for agonists compared to when they are in the inactive state, but the molecular basis for this is unclear. We have determined four active-state structures of the beta1-adrenoceptor (beta1AR) bound to conformation-specific nanobodies in the presence of agonists of varying efficacy. Comparison with inactive-state structures of beta1AR bound to the identical ligands showed a 24-42% reduction in the volume of the orthosteric binding site. Potential hydrogen bonds were also shorter, and there was up to a 30% increase in the number of atomic contacts between the receptor and ligand. This explains the increase in agonist affinity of GPCRs in the active state for a wide range of structurally distinct agonists.

Molecular basis for high-affinity agonist binding in GPCRs.,Warne T, Edwards PC, Dore AS, Leslie AGW, Tate CG Science. 2019 May 9. pii: science.aau5595. doi: 10.1126/science.aau5595. PMID:31072904[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
11 reviews cite this structure
Structure determination of GPCRs: cryo-EM compared with X-ray crystallography.
García-Nafría et al. (2021)
10 more
35 other articles
No citations found

See Also

References

  1. ↑ Warne T, Edwards PC, Dore AS, Leslie AGW, Tate CG. Molecular basis for high-affinity agonist binding in GPCRs. Science. 2019 May 9. pii: science.aau5595. doi: 10.1126/science.aau5595. PMID:31072904 doi:http://dx.doi.org/10.1126/science.aau5595

Contents


PDB ID 6h7j

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