Structural highlights
Function
MONA_DIOCU Taste-modifying protein; intensely sweet-tasting protein.MONB_DIOCU Taste-modifying protein; intensely sweet-tasting protein.
Publication Abstract from PubMed
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 beta-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 beta-hairpin proteins.
A five-residue motif for the design of domain swapping in proteins.,Nandwani N, Surana P, Negi H, Mascarenhas NM, Udgaonkar JB, Das R, Gosavi S Nat Commun. 2019 Jan 28;10(1):452. doi: 10.1038/s41467-019-08295-x. PMID:30692525[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nandwani N, Surana P, Negi H, Mascarenhas NM, Udgaonkar JB, Das R, Gosavi S. A five-residue motif for the design of domain swapping in proteins. Nat Commun. 2019 Jan 28;10(1):452. doi: 10.1038/s41467-019-08295-x. PMID:30692525 doi:http://dx.doi.org/10.1038/s41467-019-08295-x
