Molecular basis for high-affinity agonist binding in GPCRs
| Autor: | Tony Warne, Christopher G. Tate, Andrew S. Doré, Andrew G. W. Leslie, Patricia C. Edwards |
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| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Agonist Stereochemistry medicine.drug_class Plasma protein binding Ligands Protein Structure Secondary Article Receptors G-Protein-Coupled 03 medical and health sciences 0302 clinical medicine Protein structure Catalytic Domain medicine Binding site Receptor G protein-coupled receptor Multidisciplinary Hydrogen bond Chemistry Ligand Hydrogen Bonding Single-Domain Antibodies 030104 developmental biology Adrenergic beta-1 Receptor Agonists Drug Design Receptors Adrenergic beta-1 Allosteric Site 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Science. 364:775-778 |
| ISSN: | 1095-9203 0036-8075 |
| Popis: | A GPCR seen in the active state G protein–coupled receptors (GPCRs) are exceptionally good targets for drug development. Warne et al. describe four crystal structures of complexes of a GPCR—the β1-adrenergic receptor—in its active state. They used nanobodies (recombinant variable domains of heavy-chain antibodies) and engineered G protein to stabilize the β1-adrenergic receptor bound to a full agonist, two partial agonists, and a weak partial agonist. Comparison of these structures to the inactive state elucidates how agonist binding is altered in the active conformation. Science , this issue p. 775 |
| Databáze: | OpenAIRE |
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