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Title design of miniprotein agonists and antagonists targeting G protein-coupled receptors.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateJun 5, 2025
AuthorsEdin Muratspahić / David Feldman / David E Kim / Xiangli Qu / Ana-Maria Bratovianu / Paula Rivera-Sánchez / Federica Dimitri / Jason Cao / Brian P Cary / Matthew J Belousoff / Peter Keov / Qingchao Chen / Yue Ren / Justyn Fine / Isaac Sappington / Thomas Schlichthaerle / Jason Z Zhang / Arvind Pillai / Ljubica Mihaljević / Magnus Bauer / Susana Vázquez Torres / Amir Motmaen / Gyu Rie Lee / Long Tran / Xinru Wang / Inna Goreshnik / Dionne K Vafeados / Justin E Svendsen / Parisa Hosseinzadeh / Nicolai Lindegaard / Matthäus Brandt / Yann Waltenspühl / Kristine Deibler / Luke Oostdyk / William Cao / Lakshmi Anantharaman / Lance Stewart / Lauren Halloran / Jamie B Spangler / Patrick M Sexton / Bryan L Roth / Brian E Krumm / Denise Wootten / Christopher G Tate / Christoffer Norn / David Baker /
PubMed AbstractG protein-coupled receptors (GPCRs) play key roles in physiology and are central targets for drug discovery and development, yet the design of protein agonists and antagonists has been challenging as ...G protein-coupled receptors (GPCRs) play key roles in physiology and are central targets for drug discovery and development, yet the design of protein agonists and antagonists has been challenging as GPCRs are integral membrane proteins and conformationally dynamic. Here we describe computational design methods and a high throughput "receptor diversion" microscopy-based screen for generating GPCR binding miniproteins with high affinity, potency and selectivity, and the use of these methods to generate MRGPRX1 agonists and CXCR4, GLP1R, GIPR, GCGR and CGRPR antagonists. Cryo-electron microscopy data reveals atomic-level agreement between designed and experimentally determined structures for CGRPR-bound antagonists and MRGPRX1-bound agonists, confirming precise conformational control of receptor function. Our design and screening approach opens new frontiers in GPCR drug discovery and development.
External linksbioRxiv / PubMed:40501737 / PubMed Central
MethodsEM (single particle)
Resolution4.06 Å
Structure data

48424

9mni

EMDB-48424, PDB-9mni:
CGRP Receptor in complex with dC2_050
Method: EM (single particle) / Resolution: 4.06 Å

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / GPCR / de novo protein design

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