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TitleDe novo design of miniproteins targeting GPCRs.
Journal, issue, pagesNature, Year 2026
Publish dateMay 21, 2026
AuthorsEdin Muratspahić / David Feldman / David E Kim / Xiangli Qu / Ana-Maria Bratovianu / Paula Rivera-Sánchez / Jan Hendrik Voss / Emil P T Hertz / Mads Jeppesen / Federica Dimitri / Kensuke Sakamoto / Amrita Nallathambi / Pia Peceli / Jianjun Cao / Brian P Cary / Matthew J Belousoff / Peter Keov / Phuc N H Trinh / Qingchao Chen / Yue Ren / Justyn Fine / Sudha Mishra / Annu Dalal / Shachie Sinha / Ramanuj Banerjee / Manisankar Ganguly / Karthik Varappalayam Karuppusamy / Isaac Sappington / Thomas Schlichthaerle / Jason Z Zhang / Arvind Pillai / Brian Coventry / 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 / Lukas Deweid / Anja Bennett / Jendrik Schöppe / Tiantang Dong / Xiaoli Yan / Luke Oostdyk / William Cao / Lakshmi Anantharaman / Johan J Weisser / Jesper Frank Bastlund / Christoffer Bundgaard / Ayodeji A Asuni / Justin G English / Lance Stewart / Lauren Halloran / Jamie B Spangler / André Lieber / Arun K Shukla / 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, but 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, but the design of protein agonists and antagonists has been challenging as GPCRs are integral membrane proteins and conformationally dynamic. Here we describe computational de novo design methods and a high-throughput "receptor diversion" microscopy-based screen for generating GPCR binding miniproteins with high affinity, potency and selectivity. We design miniprotein agonists that activate receptors involved in itch and pain, as well as antagonists that inhibit receptors implicated in cancer, metabolic disorders such as diabetes and obesity, and migraine. Cryo-electron microscopy (cryo-EM) structures of five receptor-bound designs are close to the computational design models. A designed chemokine receptor antagonist mobilizes hematopoietic stem and progenitor cells in vivo at a level comparable to a clinically used drug, with fewer adverse effects.
External linksNature / PubMed:42168559
MethodsEM (single particle)
Resolution3.28 Å
Structure data

68747

22xc

EMDB-68747, PDB-22xc:
Structure of CXCR4 in complex with a de-novo designed mini-protein antagonist
Method: EM (single particle) / Resolution: 3.28 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

ChemComp-D21:
(2R)-1-(hexadecanoyloxy)-3-(phosphonooxy)propan-2-yl (9Z)-octadec-9-enoate

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsSIGNALING PROTEIN / GPCR / G protein / SIGNALING PROTEIN-IMMUNE SYSTEM complex

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