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Publisher Correction: Structural basis of ligand recognition at the human MT₁ melatonin receptor

Benjamin Stauch
Linda C. Johansson
Vadim Cherezov
Amendments and Corrections03 May 2019
Nature

Volume: 569, P: E6
Structural determinants of 5-HT_2B receptor activation and biased agonism

Four crystal structures of the human serotonin receptor 5-HT_2BR in complex with chemically and pharmacologically diverse drugs elucidate the structural bases for receptor activation, agonist-mediated biased signaling and β-arrestin2 translocation.

John D. McCorvy
Daniel Wacker
Bryan L. Roth
Research20 Aug 2018
Nature Structural & Molecular Biology

Volume: 25, P: 787-796
XFEL structures of the human MT₂ melatonin receptor reveal the basis of subtype selectivity

Structural and functional studies show that the MT₂ melatonin receptor, unlike the MT₁ receptor, contains an extracellular opening for ligand entry, shedding light on receptor subtype specificity.

Linda C. Johansson
Benjamin Stauch
Vadim Cherezov
Research24 Apr 2019
Nature

Volume: 569, P: 289-292
Structural basis of ligand recognition at the human MT₁ melatonin receptor

The MT₁ melatonin receptor differs markedly from 5-HT receptors and shows atypical ligand entry; its structure with various ligands sheds light on receptor specificity.

Benjamin Stauch
Linda C. Johansson
Vadim Cherezov
Research24 Apr 2019
Nature

Volume: 569, P: 284-288

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Publisher Correction: Structural basis of ligand recognition at the human MT1 melatonin receptor

Structural determinants of 5-HT2B receptor activation and biased agonism

XFEL structures of the human MT2 melatonin receptor reveal the basis of subtype selectivity

Structural basis of ligand recognition at the human MT1 melatonin receptor

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Publisher Correction: Structural basis of ligand recognition at the human MT₁ melatonin receptor

Structural determinants of 5-HT_2B receptor activation and biased agonism

XFEL structures of the human MT₂ melatonin receptor reveal the basis of subtype selectivity

Structural basis of ligand recognition at the human MT₁ melatonin receptor