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

Structure-inspired design of β-arrestin-biased ligands for aminergic GPCRs.

Nature chemical biology - 1 Feb 2018

McCorvy John D, Butler Kyle V, Kelly Brendan, Rechsteiner Katie, Karpiak Joel, Betz Robin M, Kormos Bethany L, Shoichet Brian K, Dror Ron O, Jin Jian, Roth Bryan L

Abstract excerpt

Development of biased ligands targeting G protein-coupled receptors (GPCRs) is a promising approach for current drug discovery. Although structure-based drug design of biased agonists remains challenging even with an abundance of GPCR crystal structures, we present an approach for translating GPCR structural data into β-arrestin-biased ligands for aminergic GPCRs. We identified specific amino acid-ligand contacts...

Read the complete abstract on PubMed

Topics

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

Share to Cyclic AMP
Share to Drug Design

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Discovery

Share to Hydrogen Bonding

Share to Indoles

Share to Molecular Dynamics Simulation

Share to Receptors, G-Protein-Coupled

Share to Serine

Source

Open in PubMed Open full text

Identifiers

PMID: 29227473
DOI: 10.1038/nchembio.2527
PMCID: PMC5771956

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure-inspired design of β-arrestin-biased ligands for aminergic GPCRs.PMID 29227473Read ↗

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

β-Arrestins and disease-linked variants: opportunities for targeted modulation.Semantic proximity Read ↗

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

Biased signaling in naturally occurring mutations of G protein-coupled receptors associated with diverse human diseases.Semantic proximity Read ↗

Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins.Semantic proximity Read ↗

β2 -Adrenoceptor agonist profiling reveals biased signalling phenotypes for the β2 -adrenoceptor with possible implications for the treatment of asthma.Semantic proximity Read ↗

Hidden Bias: GPCR Polymorphisms and the Genomic Landscape of β-Arrestin SignalingSemantic proximity Read ↗

Key aspects of modern GPCR drug discoverySemantic proximity Read ↗

The GLP-1R as a model for understanding and exploiting biased agonism in next-generation medicinesSemantic proximity Read ↗

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

Characterizing the role of extracellular domain in GLP-1R biased agonism.Semantic proximity Read ↗

Bravizine: A β-Arrestin–Biased Partial Agonist Targeting Dopamine D2 Receptor Hypersensitivity in Tardive DyskinesiaSemantic proximity Read ↗

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