Structural snapshot of a β-arrestin-biased receptor

Parishmita Sarma; Ramanuj Banerjee; Arun K Shukla

doi:10.1016/j.tips.2022.08.005

Structural snapshot of a β-arrestin-biased receptor

Trends Pharmacol Sci. 2023 Jan;44(1):1-3. doi: 10.1016/j.tips.2022.08.005. Epub 2022 Aug 31.

Authors

Parishmita Sarma¹, Ramanuj Banerjee¹, Arun K Shukla²

Affiliations

¹ Department of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur 208016, India.
² Department of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur 208016, India. Electronic address: arshukla@iitk.ac.in.

Abstract

Atypical chemokine receptor subtype 3 (ACKR3), a chemokine receptor, couples selectively to β-arrestins (βarrs) but not to G proteins despite having seven transmembrane (7TM) helix architecture. Yen et al. present cryogenic-electron microscopy (cryo-EM) structures of agonist-bound ACKR3, elucidating a distinct chemokine-binding mechanism, and offering a structural template to probe the transducer-coupling bias at this receptor.

Keywords: ACKR3; ACRs; GPCRs; biased agonism; chemokines; intrinsic bias; β-arrestins.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Humans
Protein Binding
Receptors, CXCR* / chemistry
Signal Transduction*
beta-Arrestins* / chemistry

Substances

beta-Arrestins
ACKR3 protein, human
Receptors, CXCR

Abstract

Publication types

MeSH terms

Substances

Grants and funding