TitleAmino-acid composition after loop deletion drives domain swapping.
Publication TypeJournal Article
Year of Publication2017
AuthorsNandwani N, Surana P, Udgaonkar JB, Das R, Gosavi S
JournalProtein Sci
Volume26
Issue10
Start Page1994
Date Published10/2017
ISSN1469-896X
Abstract

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.

DOI10.1002/pro.3237
Alternate JournalProtein Sci.
PubMed ID28710790