KRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe

Mutant RAS family members occur in a wide range of tumour types, and there is a great interest in identifying isoform-specific inhibitors. Here, the authors characterise two designed ankyrin repeat proteins (DARPins) that specifically inhibit the KRAS isoform by binding to the region around the KRAS...

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Autores principales: Nicolas Bery, Sandrine Legg, Judit Debreczeni, Jason Breed, Kevin Embrey, Christopher Stubbs, Paulina Kolasinska-Zwierz, Nathalie Barrett, Rose Marwood, Jo Watson, Jon Tart, Ross Overman, Ami Miller, Christopher Phillips, Ralph Minter, Terence H. Rabbitts
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Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/d60832bba2a448e1bd87fa3edb2b14fd
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spelling oai:doaj.org-article:d60832bba2a448e1bd87fa3edb2b14fd2021-12-02T17:32:40ZKRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe10.1038/s41467-019-10419-22041-1723https://doaj.org/article/d60832bba2a448e1bd87fa3edb2b14fd2019-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10419-2https://doaj.org/toc/2041-1723Mutant RAS family members occur in a wide range of tumour types, and there is a great interest in identifying isoform-specific inhibitors. Here, the authors characterise two designed ankyrin repeat proteins (DARPins) that specifically inhibit the KRAS isoform by binding to the region around the KRAS-specific residue histidine 95 and show that they affect KRAS/effector interactions in different ways.Nicolas BerySandrine LeggJudit DebreczeniJason BreedKevin EmbreyChristopher StubbsPaulina Kolasinska-ZwierzNathalie BarrettRose MarwoodJo WatsonJon TartRoss OvermanAmi MillerChristopher PhillipsRalph MinterTerence H. RabbittsNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Nicolas Bery
Sandrine Legg
Judit Debreczeni
Jason Breed
Kevin Embrey
Christopher Stubbs
Paulina Kolasinska-Zwierz
Nathalie Barrett
Rose Marwood
Jo Watson
Jon Tart
Ross Overman
Ami Miller
Christopher Phillips
Ralph Minter
Terence H. Rabbitts
KRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe
description Mutant RAS family members occur in a wide range of tumour types, and there is a great interest in identifying isoform-specific inhibitors. Here, the authors characterise two designed ankyrin repeat proteins (DARPins) that specifically inhibit the KRAS isoform by binding to the region around the KRAS-specific residue histidine 95 and show that they affect KRAS/effector interactions in different ways.
format article
author Nicolas Bery
Sandrine Legg
Judit Debreczeni
Jason Breed
Kevin Embrey
Christopher Stubbs
Paulina Kolasinska-Zwierz
Nathalie Barrett
Rose Marwood
Jo Watson
Jon Tart
Ross Overman
Ami Miller
Christopher Phillips
Ralph Minter
Terence H. Rabbitts
author_facet Nicolas Bery
Sandrine Legg
Judit Debreczeni
Jason Breed
Kevin Embrey
Christopher Stubbs
Paulina Kolasinska-Zwierz
Nathalie Barrett
Rose Marwood
Jo Watson
Jon Tart
Ross Overman
Ami Miller
Christopher Phillips
Ralph Minter
Terence H. Rabbitts
author_sort Nicolas Bery
title KRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe
title_short KRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe
title_full KRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe
title_fullStr KRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe
title_full_unstemmed KRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe
title_sort kras-specific inhibition using a darpin binding to a site in the allosteric lobe
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/d60832bba2a448e1bd87fa3edb2b14fd
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