Structural highlights
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.
See Also
References
- ↑ 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
