
@article {50995,
	title = {A five-residue motif for the design of domain swapping in proteins.},
	journal = {Nat Commun},
	volume = {10},
	year = {2019},
	month = {2019 01 28},
	pages = {452},
	abstract = {<p>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 {\textquoteright}cystatin motif{\textquoteright} (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.</p>
},
	issn = {2041-1723},
	doi = {10.1038/s41467-019-08295-x},
	author = {Nandwani, Neha and Surana, Parag and Negi, Hitendra and Mascarenhas, Nahren M and Udgaonkar, Jayant B and Das, Ranabir and Gosavi, Shachi}
}
@article {20316,
	title = {Amino-acid composition after loop deletion drives domain swapping.},
	journal = {Protein Sci},
	volume = {26},
	year = {2017},
	month = {10/2017},
	chapter = {1994},
	abstract = {<p>Rational engineering of a protein to enable domain swapping requires an understanding of the sequence, structural and energetic factors that favor the domain-swapped oligomer over the monomer. While it is known that the deletion of loops between β-strands can promote domain swapping, the spliced sequence at the position of the loop deletion is thought to have a minimal role to play in such domain swapping. Here, two loop-deletion mutants of the non-domain-swapping protein monellin, frame-shifted by a single residue, were designed. Although the spliced sequence in the two mutants differed by only one residue at the site of the deletion, only one of them (YEIKG) promoted domain swapping. The mutant containing the spliced sequence YENKG was entirely monomeric. This new understanding that the domain swapping propensity after loop deletion may depend critically on the chemical composition of the shortened loop will facilitate the rational design of domain swapping. This article is protected by copyright. All rights reserved.</p>
},
	issn = {1469-896X},
	doi = {10.1002/pro.3237},
	author = {Nandwani, Neha and Surana, Parag and Udgaonkar, Jayant B and Das, Ranabir and Gosavi, Shachi}
}
