ArticleProtein science : a publication of the Protein Society2017
Amino-acid composition after loop deletion drives domain swapping.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- The pedal-like loop of (R)-selective transaminases plays a critical role to the functionality of the enzyme.Biotechnology letters · 2025Article
- Experimental and theoretical study on converting myoglobin into a stable domain-swapped dimer by utilizing a tight hydrogen bond network at the hinge region.RSC advances · 2021Article
- Structural basis of dimerization and dual W-box DNA recognition by rice WRKY domain.Nucleic acids research · 2019Article
- A five-residue motif for the design of domain swapping in proteins.Nature communications · 2019Article
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5 authors.
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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.
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