Structural highlights
6h7l is a 6 chain structure with sequence from Camelus glama, Ecoli and Melga. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| Gene: | trxA, fipA, tsnC, b3781, JW5856 (ECOLI), ADRB1 (MELGA) |
| 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. [ADRB1_MELGA] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity.
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
