The Design of Metal Ion‐Induced Dimers Suggestive of 3D Domain Swapping
and the histidine residues within the His-Pro repeats. This predicted structure remained stable during 100-ns molecular dynamics simulations. These experimental and computational evaluations suggest that the insertion of His-Pro repeats into loops is an effective strategy for designing metal ion-induced dimers suggestive of 3D domain-swapped dimers. Our results provide insights into expanding the design space of artificial metal ion-dependent protein dimers and advancing our understanding of the structural principles of metalloproteins.
Authors
- Kenta Hongo (ORCID: https://orcid.org/0000-0002-2580-0907)
- Norio Yoshida (ORCID: https://orcid.org/0000-0002-2023-7254)
- Kodai Kanemaru (ORCID: https://orcid.org/0009-0007-3211-735X)
- Shota Shiga
- Koki Makabe (ORCID: https://orcid.org/0000-0003-3168-8445)
- Seiya Sugiyama
- Satoshi Ito
Institutions
- Yamagata University (JP)
- Japan Advanced Institute of Science and Technology (JP)
- Kyoto University (JP)
- Nagoya University (JP)
Publication Details
- Journal
- ChemBioChem
- Published
- 2026-04-30
- DOI
- https://doi.org/10.1002/cbic.70363
- Primary Topic
- Protein Structure and Dynamics
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Japan Society for the Promotion of Science
- Japan Science and Technology Agency