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TitleDevelopment of an allosteric adhesion GPCR nanobody with therapeutic potential.
Journal, issue, pagesNat Chem Biol, Vol. 21, Issue 10, Page 1519-1530, Year 2025
Publish dateMay 15, 2025
AuthorsYuan Zheng / Dan Jiang / Yan Lu / Chao Zhang / Shen-Ming Huang / Haocheng Lin / Daolai Zhang / Shengchao Guo / Jifei Han / Jun Chen / Yaxuan He / Mingxiang Zhang / Yanhui Gao / Yongyuan Guo / Ran Wei / Ming Xia / Yingying Qin / Zhaoqian Liu / Fan Yang / Shaohua Ge / Fan Yi / Xiao Yu / Hui Lin / Peng Xiao / Jin-Peng Sun / Shiqing Feng /
PubMed AbstractAllosteric modulation of receptor responses to endogenous agonists has therapeutic value, maintaining ligand profiles, reducing side effects and restoring mutant responses. Adhesion G-protein-coupled ...Allosteric modulation of receptor responses to endogenous agonists has therapeutic value, maintaining ligand profiles, reducing side effects and restoring mutant responses. Adhesion G-protein-coupled receptors (aGPCRs), with large N termini, are ideal for allosteric modulator development. We designed a nanobody strategy targeting ADGRG2 N-terminal fragments and got a specific nanobody Nb23-bi, which promoted dehydroepiandrosterone (DHEA)-induced ADGRG2 activation and reversed mutant-induced dysfunctions. By combining structural characterization, crosslinking mass spectrometry, mutational analysis and molecular dynamics simulations, we clarified the allosteric mechanism of how the Nb23-bi modulates conformational changes in the DHEA-binding pocket. Animal studies showed that Nb23-bi promoted the response of DHEA in alleviating testicular inflammation and reversing mutant defects. In summary, we developed an allosteric nanobody of ADGRG2 and gained insights into its functions in reversing disease-associated dysfunctions. Our study may serve as a template for developing allosteric modulators of other aGPCRs for biological and therapeutic purposes.
External linksNat Chem Biol / PubMed:40374856
MethodsEM (single particle)
Resolution2.9 Å
Structure data

39365

8ykd

EMDB-39365, PDB-8ykd:
Cryo-EM structure of ADGRG2-Gs complex with NTF nanobody
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-AND:
3-BETA-HYDROXY-5-ANDROSTEN-17-ONE / hormone*YM

Source
  • Bos taurus (domestic cattle)
  • spodoptera (butterflies/moths)
KeywordsMEMBRANE PROTEIN / GPCR

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