A five-residue motif for the design of domain swapping in proteins

Neha Nandwani, Parag Surana, Hitendra Negi, Nahren M. Mascarenhas, Jayant B. Udgaonkar (), Ranabir Das () and Shachi Gosavi ()
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Neha Nandwani: Tata Institute of Fundamental Research
Parag Surana: Tata Institute of Fundamental Research
Hitendra Negi: Tata Institute of Fundamental Research
Nahren M. Mascarenhas: Tata Institute of Fundamental Research
Jayant B. Udgaonkar: Tata Institute of Fundamental Research
Ranabir Das: Tata Institute of Fundamental Research
Shachi Gosavi: Tata Institute of Fundamental Research

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: Abstract Domain swapping is the process by which identical monomeric proteins exchange structural elements to generate dimers/oligomers. Although engineered domain swapping is a compelling strategy for protein assembly, its application has been limited due to the lack of simple and reliable design approaches. Here, we demonstrate that the hydrophobic five-residue ‘cystatin motif’ (QVVAG) from the domain-swapping protein Stefin B, when engineered into a solvent-exposed, tight surface loop between two β-strands prevents the loop from folding back upon itself, and drives domain swapping in non-domain-swapping proteins. High-resolution structural studies demonstrate that engineering the QVVAG stretch independently into various surface loops of four structurally distinct non-domain-swapping proteins enabled the design of different modes of domain swapping in these proteins, including single, double and open-ended domain swapping. These results suggest that the introduction of the QVVAG motif can be used as a mutational approach for engineering domain swapping in diverse β-hairpin proteins.

Date: 2019
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DOI: 10.1038/s41467-019-08295-x

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