Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A structural basis for how ligand binding site changes can allosterically regulate GPCR signaling and engender functional selectivity.

Science signaling - 4 Feb 2020

Sanchez-Soto Marta, Verma Ravi Kumar, Willette Blair K A, Gonye Elizabeth C, Moore Annah M, Moritz Amy E, Boateng Comfort A, Yano Hideaki, Free R Benjamin, Shi Lei, Sibley David R

Abstract excerpt

Signaling bias is the propensity for some agonists to preferentially stimulate G protein-coupled receptor (GPCR) signaling through one intracellular pathway versus another. We previously identified a G protein-biased agonist of the D2 dopamine receptor (D2R) that results in impaired β-arrestin recruitment. This signaling bias was predicted to arise from unique interactions of the ligand with a hydrophobic pocket...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to beta-Arrestins
Share to CHO Cells

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cricetulus

Share to GTP-Binding Proteins

Share to Molecular Dynamics Simulation

Share to Protein Domains

Share to Receptors, Adrenergic, beta-2

Share to Receptors, G-Protein-Coupled

Source

Open in PubMed Open full text

Identifiers

PMID: 32019899
DOI: 10.1126/scisignal.aaw5885
PMCID: PMC7236428

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A structural basis for how ligand binding site changes can allosterically regulate GPCR signaling and engender functional selectivity.PMID 32019899Read ↗

Structure-inspired design of β-arrestin-biased ligands for aminergic GPCRs.Semantic proximity Read ↗

Interhelical interaction and receptor phosphorylation regulate the activation kinetics of different human β1-adrenoceptor variants.Semantic proximity Read ↗

Computational design of constitutively active mutants of Dopamine D2 receptor inspired by ligand-independent activation mechanisms.Semantic proximity Read ↗

Distinct CCK-2 receptor conformations associated with β-arrestin-2 recruitment or phospholipase-C activation revealed by a biased antagonist.Semantic proximity Read ↗

Evolutionary action and structural basis of the allosteric switch controlling β2AR functional selectivity.Semantic proximity Read ↗

A small molecule enhances arrestin-3 binding to the β <sub>2</sub> -adrenergic receptorSemantic proximity Read ↗

The dopamine D2 receptor can directly recruit and activate GRK2 without G protein activation.Semantic proximity Read ↗

GPCR-MAPS: high-resolution functional and allosteric mapping of G protein-coupled receptor activation and biasSemantic proximity Read ↗

The structural determinants of the bitopic binding mode of a negative allosteric modulator of the dopamine D2 receptor.Semantic proximity Read ↗

Structural dynamics and energetics underlying allosteric inactivation of the cannabinoid receptor CB1.Semantic proximity Read ↗

Engineering a GPCR-ligand pair that simulates the activation of D(2L) by Dopamine.Semantic proximity Read ↗

Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.