dc.contributor.author |
Nandwani, Neha |
en_US |
dc.contributor.author |
Surana, Parag |
en_US |
dc.contributor.author |
Negi, Hitendra |
en_US |
dc.contributor.author |
Mascarenhas, Nahren M. |
en_US |
dc.contributor.author |
UDGAONKAR, JAYANT B. |
en_US |
dc.contributor.author |
Das, Ranabir |
en_US |
dc.contributor.author |
Gosavi, Shachi |
en_US |
dc.date.accessioned |
2019-02-18T04:04:03Z |
|
dc.date.available |
2019-02-18T04:04:03Z |
|
dc.date.issued |
2019-01 |
en_US |
dc.identifier.citation |
Nature Communications, 10. |
en_US |
dc.identifier.issn |
2041-1723 |
en_US |
dc.identifier.uri |
http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/1892 |
|
dc.identifier.uri |
https://doi.org/10.1038/s41467-019-08295-x |
en_US |
dc.description.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. |
en_US |
dc.language.iso |
en |
en_US |
dc.publisher |
Nature Publishing Group |
en_US |
dc.subject |
Biophysical chemistry |
en_US |
dc.subject |
Protein folding |
en_US |
dc.subject |
SAXS |
en_US |
dc.subject |
Solution-state NMR |
en_US |
dc.subject |
X-ray crystallography |
en_US |
dc.subject |
TOC-FEB-2019 |
en_US |
dc.subject |
2019 |
en_US |
dc.title |
A five-residue motif for the design of domain swapping in proteins |
en_US |
dc.type |
Article |
en_US |
dc.contributor.department |
Dept. of Biology |
en_US |
dc.identifier.sourcetitle |
Nature Communications |
en_US |
dc.publication.originofpublisher |
Foreign |
en_US |