Matches in SemOpenAlex for { <https://semopenalex.org/work/W2913133800> ?p ?o ?g. }
- W2913133800 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." @default.
- W2913133800 created "2019-02-21" @default.
- W2913133800 creator A5005570919 @default.
- W2913133800 creator A5034743915 @default.
- W2913133800 creator A5056115805 @default.
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- W2913133800 creator A5057549416 @default.
- W2913133800 creator A5076925232 @default.
- W2913133800 creator A5087725258 @default.
- W2913133800 date "2019-01-28" @default.
- W2913133800 modified "2023-10-13" @default.
- W2913133800 title "A five-residue motif for the design of domain swapping in proteins" @default.
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- W2913133800 doi "https://doi.org/10.1038/s41467-019-08295-x" @default.
- W2913133800 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6349918" @default.
- W2913133800 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30692525" @default.
- W2913133800 hasPublicationYear "2019" @default.
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