8UDN
A Stable Heterotrimeric Foldon with Minimum Mutation
Summary for 8UDN
| Entry DOI | 10.2210/pdb8udn/pdb |
| Descriptor | Fibritin (2 entities in total) |
| Functional Keywords | foldon heterotrimer self-assembly peptides miniprotein, viral protein |
| Biological source | Tequatrovirus T4 |
| Total number of polymer chains | 3 |
| Total formula weight | 9388.56 |
| Authors | Bingman, C.A.,Liu, X.,Roberts, D.S.,Gellman, S.H. (deposition date: 2023-09-28, release date: 2025-05-14, Last modification date: 2025-07-23) |
| Primary citation | Liu, X.,Roberts, D.S.,Bingman, C.A.,Ge, Y.,Gellman, S.H. Rational Design of a Foldon-Derived Heterotrimer Guided by Quantitative Native Mass Spectrometry. J.Am.Chem.Soc., 147:23819-23826, 2025 Cited by PubMed Abstract: Designing stable hetero-oligomeric protein complexes with defined intersubunit stoichiometry remains a significant challenge. In this study, we report the design of a highly selective heterotrimeric assembly derived from the well-known foldon homotrimer. We generated an heterotrimer by replacing glutamine 11 with glutamic acid, to destabilize the homotrimer, and replacing valine 14 with either alanine or leucine, to stabilize the hydrophobic core of the heterotrimer. Native mass spectrometry (MS) was essential for guiding the design process, enabling precise characterization of oligomeric states and their equilibrium distributions. The heterotrimer structure was validated by X-ray crystallography. Our findings highlight the effectiveness of combining rational design with native MS to develop specific hetero-oligomeric assemblies. PubMed: 40580137DOI: 10.1021/jacs.5c06094 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.97 Å) |
Structure validation
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