Back

Collaborative multi-agent intelligence uncovers subtype-selective allosteric sites at GPCR-lipid interaction interface

Zhu, J.; Li, H.; Xiao, M.; Wang, L.; Jiang, X.

2026-08-07 biochemistry
10.64898/2026.08.06.743397 bioRxiv
Show abstract

Closely related G protein-coupled receptor (GPCR) subtypes often share highly conserved orthosteric pockets, making subtype-selective ligand development challenging. Here, we developed a five-agent workflow to systematically identify divergent protein-membrane-interface sites across class A GPCRs and exploit them for selective allosteric ligand discovery. By combining dMaSIF-derived surface fingerprints with Ballesteros-Weinstein (BW) position alignment, we compared structurally equivalent membrane-facing regions and identified the three most divergent hotspots for each of 163 receptor pairs. These regions showed substantial spatial overlap with experimentally characterized allosteric sites. Paired target-off-target screening of one million lead-like compounds, followed by detail-mode redocking and multi-seed consistency filtering, yielded 352 receptor-pair-specific candidates corresponding to 344 unique compounds across 104 receptor pairs. These candidates, together with their divergent sites and predicted selectivity profiles, were integrated into a searchable database. Our findings establish a scalable strategy for translating GPCR membrane-interface divergence into precise allosteric sites and testable subtype-selective ligand candidates.

Matching journals

The top 5 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.