Proteomics

Dataset Information

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Conformational dynamics underlying Atypical Chemokine Receptor 3 activation

ABSTRACT: Here we used Hydrogen/Deuterium exchange mass spectrometry (HDX-MS) to examine the binding mode and mechanism of action of various small-molecule ACKR3 ligands of different efficacy for β-arrestin recruitment. Our results show that activation or inhibition of ACKR3 is largely governed by intracellular conformational changes of helix 6, intracellular loop 2 and helix 7, while the DRY motif becomes protected during both processes. Moreover, HDX-MS identifies the binding sites and the allosteric modulation of ACKR3 upon β-arrestin 1 binding.

INSTRUMENT(S): nanoACQUITY UPLC with HDX Technology

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Functional Proteomics Platform FPP  

LAB HEAD: Cherine Bechara

PROVIDER: PXD044103 | Pride | 2024-07-16

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
ACKR3_sequence.txt Txt
Dataset1_arrestin-Dataset2_15485_25550.tar.bz2 Other
Dataset1_small-ligands.tar.bz2 Other
Dataset2_16840.tar.bz2 Other
Dataset2_arrestin.tar.bz2 Other
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Publications

Conformational dynamics underlying atypical chemokine receptor 3 activation.

Otun Omolade O   Aljamous Christelle C   Del Nero Elise E   Arimont-Segura Marta M   Bosma Reggie R   Zarzycka Barbara B   Girbau Tristan T   Leyrat Cédric C   de Graaf Chris C   Leurs Rob R   Durroux Thierry T   Granier Sébastien S   Cong Xiaojing X   Bechara Cherine C  

Proceedings of the National Academy of Sciences of the United States of America 20240715 30

Atypical Chemokine Receptor 3 (ACKR3) belongs to the G protein-coupled receptor family but it does not signal through G proteins. The structural properties that govern the functional selectivity and the conformational dynamics of ACKR3 activation are poorly understood. Here, we combined hydrogen/deuterium exchange mass spectrometry, site-directed mutagenesis, and molecular dynamics simulations to examine the binding mode and mechanism of action of ACKR3 ligands of different efficacies. Our resul  ...[more]

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