A five-residue motif for the design of domain swapping in proteins

A five-residue motif for the design of domain swapping in proteins

Designing interfaces that can induce protein-protein interactions is a challenging problem. Here the authors show that a five amino acid sequence known to mediate domain swapping in cystatins can drive oligomerization when grafted onto functionally and structurally unrelated host proteins, providing...

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Main Authors: Neha Nandwani, Parag Surana, Hitendra Negi, Nahren M. Mascarenhas, Jayant B. Udgaonkar, Ranabir Das, Shachi Gosavi
Format: Article
Language:English
Published: Nature Publishing Group 2019-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-08295-x
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spelling doaj-9b6bdc87e3ab4b35a3fc024b6c07e9142021-05-11T12:40:29ZengNature Publishing GroupNature Communications2041-17232019-01-0110111310.1038/s41467-019-08295-xA five-residue motif for the design of domain swapping in proteinsNeha Nandwani0Parag Surana1Hitendra Negi2Nahren M. Mascarenhas3Jayant B. Udgaonkar4Ranabir Das5Shachi Gosavi6National Centre for Biological Sciences, Tata Institute of Fundamental ResearchNational Centre for Biological Sciences, Tata Institute of Fundamental ResearchNational Centre for Biological Sciences, Tata Institute of Fundamental ResearchNational Centre for Biological Sciences, Tata Institute of Fundamental ResearchNational Centre for Biological Sciences, Tata Institute of Fundamental ResearchNational Centre for Biological Sciences, Tata Institute of Fundamental ResearchNational Centre for Biological Sciences, Tata Institute of Fundamental ResearchDesigning interfaces that can induce protein-protein interactions is a challenging problem. Here the authors show that a five amino acid sequence known to mediate domain swapping in cystatins can drive oligomerization when grafted onto functionally and structurally unrelated host proteins, providing a simple approach to the design of protein assemblies.https://doi.org/10.1038/s41467-019-08295-x
collection DOAJ
language English
format Article
sources DOAJ
author Neha Nandwani
Parag Surana
Hitendra Negi
Nahren M. Mascarenhas
Jayant B. Udgaonkar
Ranabir Das
Shachi Gosavi
spellingShingle Neha Nandwani
Parag Surana
Hitendra Negi
Nahren M. Mascarenhas
Jayant B. Udgaonkar
Ranabir Das
Shachi Gosavi
A five-residue motif for the design of domain swapping in proteins
Nature Communications
author_facet Neha Nandwani
Parag Surana
Hitendra Negi
Nahren M. Mascarenhas
Jayant B. Udgaonkar
Ranabir Das
Shachi Gosavi
author_sort Neha Nandwani
title A five-residue motif for the design of domain swapping in proteins
title_short A five-residue motif for the design of domain swapping in proteins
title_full A five-residue motif for the design of domain swapping in proteins
title_fullStr A five-residue motif for the design of domain swapping in proteins
title_full_unstemmed A five-residue motif for the design of domain swapping in proteins
title_sort five-residue motif for the design of domain swapping in proteins
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-01-01
description Designing interfaces that can induce protein-protein interactions is a challenging problem. Here the authors show that a five amino acid sequence known to mediate domain swapping in cystatins can drive oligomerization when grafted onto functionally and structurally unrelated host proteins, providing a simple approach to the design of protein assemblies.
url https://doi.org/10.1038/s41467-019-08295-x
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