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PubMed · 12869697

Long-distance conformational changes in a protein engineered by modulated sequence duplication.

Martin Sagermann·Leslie Gay·Brian W Matthews
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Abstract

There are few, if any, known instances in which a biological signal is transmitted via a large conformational change through the body of a protein. We describe here a mutant of T4 lysozyme that was engineered to permit structural change at a distance. The design uses a tandem sequence repeat that makes it possible to transmit large-scale structural changes from one end of an alpha-helix to the other over a distance of 17-25 A. The method should be of general applicability and may make it possible to introduce a mutation at one site in a protein that will induce large-scale changes in the structure at a spatially remote site.

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Binding SitesCrystallography, X-RayGlycineModels, MolecularMuramidaseMutagenesisMutationPeptide FragmentsPeptidesProtein ConformationProtein Structure, TertiaryJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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Martin Sagermann, Leslie Gay, Brian W Matthews. 2003-07-17. Long-distance conformational changes in a protein engineered by modulated sequence duplication.. https://doi.org/10.1073/pnas.1633549100

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