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Structure paper

TitleStructural basis of β-arrestin coupling and transducer selectivity in PAC1R.
Journal, issue, pagesActa Pharmacol Sin, Year 2026
Publish dateSep 8, 2026
AuthorsMin Zhang / Xin Li / Qing-Ning Yuan / Wen Hu / H Eric Xu / Li-Hua Zhao /
PubMed AbstractThe pituitary adenylate cyclase-activating polypeptide receptor (PAC1R) is a class B G protein-coupled receptor (GPCR) that engages both G proteins and β-arrestins to mediate diverse signaling ...The pituitary adenylate cyclase-activating polypeptide receptor (PAC1R) is a class B G protein-coupled receptor (GPCR) that engages both G proteins and β-arrestins to mediate diverse signaling responses, yet how PAC1R adopts distinct intracellular conformations to achieve this transducer selectivity remains poorly understood. Here, we report the cryo-electron microscopy structure of PAC1R in complex with β-arrestin 1 (βarr1), revealing a core-engaged conformation. Comparison with the G-bound PAC1R structure shows that βarr1 engagement is associated with remodeling of the intracellular transmembrane bundle, including TM5 reorientation and inward movement of TM6, resulting in a receptor core geometry distinct from that of the G protein-bound state. Comparison with the βarr1-bound parathyroid hormone receptor 1 (PTH1R) structure further reveals both conserved and receptor-specific features of βarr1 engagement. Although outward displacement of the TM5 cytoplasmic end is observed in both PAC1R-βarr1 and PTH1R-βarr1 complexes, its specific direction and the resulting TM5-TM6 rearrangements differ between receptors, correlating with distinct βarr1 finger loop orientations within the receptor core. Together, these findings suggest that β-arrestin core engagement by class B GPCRs is accompanied by receptor-specific intracellular remodeling that may contribute to transducer selectivity in PAC1R.
External linksActa Pharmacol Sin / PubMed:42706324
MethodsEM (single particle)
Resolution3.0 - 3.56 Å
Structure data

EMDB-81088: A consensus Cryo_EM structure of PACAP27_PAC1R_Beta_arrestin 1 complex
Method: EM (single particle) / Resolution: 3.09 Å

EMDB-81089: A focused Cryo_EM structure of PAC1R of PACAP27_PAC1R_Beta_arrestin 1 complex
Method: EM (single particle) / Resolution: 3.56 Å

EMDB-81091: A focused Cryo_EM structure of Arrestin of PACAP27_PAC1R_Beta_arrestin 1 complex
Method: EM (single particle) / Resolution: 3.01 Å

81097

27em

EMDB-81097, PDB-27em:
Cryo_EM structure of PACAP27_PAC1R_Beta_arrestin 1 complex
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN/IMMUNE SYSTEM / GPCR / Beta arrestin1 / MEMBRANE PROTEIN-IMMUNE SYSTEM complex

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