It was unknown whether the intrinsically disordered region of IL2RG could be specifically targeted by designed binders; RFdiffusion-generated binders demonstrated that this IDR adopts a beta-strand conformation amenable to high-affinity binding, establishing a new modality for modulating IL-2 signaling at the receptor level.
Evidence Computational binder design (RFdiffusion) with biophysical affinity measurement (10–100 nM Kd) and cellular colocalization imaging (preprint)
PMID:bio_10.1101_2024.07.16.603789
- Single preprint without peer review or independent replication
- No mechanistic dissection of how binder engagement alters downstream JAK-STAT signaling
- Structural basis of the IDR beta-strand conformation not resolved at atomic level