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Self-assembly and regulation of protein cages from pre-organised coiled-coil modules

Author

Listed:
  • Fabio Lapenta

    (National Institute of Chemistry
    EN-FIST Centre of Excellence)

  • Jana Aupič

    (National Institute of Chemistry)

  • Marco Vezzoli

    (University of Parma)

  • Žiga Strmšek

    (National Institute of Chemistry)

  • Stefano Da Vela

    (EMBL c/o DESY)

  • Dmitri I. Svergun

    (EMBL c/o DESY)

  • José María Carazo

    (Centro Nacional de Biotecnología (CNB-CSIC))

  • Roberto Melero

    (Centro Nacional de Biotecnología (CNB-CSIC))

  • Roman Jerala

    (National Institute of Chemistry
    EN-FIST Centre of Excellence)

Abstract

Coiled-coil protein origami (CCPO) is a modular strategy for the de novo design of polypeptide nanostructures. CCPO folds are defined by the sequential order of concatenated orthogonal coiled-coil (CC) dimer-forming peptides, where a single-chain protein is programmed to fold into a polyhedral cage. Self-assembly of CC-based nanostructures from several chains, similarly as in DNA nanotechnology, could facilitate the design of more complex assemblies and the introduction of functionalities. Here, we show the design of a de novo triangular bipyramid fold comprising 18 CC-forming segments and define the strategy for the two-chain self-assembly of the bipyramidal cage from asymmetric and pseudo-symmetric pre-organised structural modules. In addition, by introducing a protease cleavage site and masking the interfacial CC-forming segments in the two-chain bipyramidal cage, we devise a proteolysis-mediated conformational switch. This strategy could be extended to other modular protein folds, facilitating the construction of dynamic multi-chain CC-based complexes.

Suggested Citation

  • Fabio Lapenta & Jana Aupič & Marco Vezzoli & Žiga Strmšek & Stefano Da Vela & Dmitri I. Svergun & José María Carazo & Roberto Melero & Roman Jerala, 2021. "Self-assembly and regulation of protein cages from pre-organised coiled-coil modules," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21184-6
    DOI: 10.1038/s41467-021-21184-6
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    Cited by:

    1. Estera Merljak & Benjamin Malovrh & Roman Jerala, 2023. "Segmentation strategy of de novo designed four-helical bundles expands protein oligomerization modalities for cell regulation," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Sicong Yao & Adam Moyer & Yiwu Zheng & Yang Shen & Xiaoting Meng & Chong Yuan & Yibing Zhao & Hongwei Yao & David Baker & Chuanliu Wu, 2022. "De novo design and directed folding of disulfide-bridged peptide heterodimers," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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