Domain-interface dynamics of CFTR revealed by stabilizing nanobodies

The leading cause of cystic fibrosis is the deletion of phenylalanine 508 (F508del) in the first nucleotide-binding domain (NBD1) of the cystic fibrosis transmembrane conductance regulator (CFTR). Here authors we develop nanobodies targeting NBD1 of human CFTR and demonstrate their ability to stabil...

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Autores principales: Maud Sigoillot, Marie Overtus, Magdalena Grodecka, Daniel Scholl, Abel Garcia-Pino, Toon Laeremans, Lihua He, Els Pardon, Ellen Hildebrandt, Ina Urbatsch, Jan Steyaert, John R. Riordan, Cedric Govaerts
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Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/2a36a5cc137946bdbc014d5d58e302cb
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spelling oai:doaj.org-article:2a36a5cc137946bdbc014d5d58e302cb2021-12-02T16:57:30ZDomain-interface dynamics of CFTR revealed by stabilizing nanobodies10.1038/s41467-019-10714-y2041-1723https://doaj.org/article/2a36a5cc137946bdbc014d5d58e302cb2019-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10714-yhttps://doaj.org/toc/2041-1723The leading cause of cystic fibrosis is the deletion of phenylalanine 508 (F508del) in the first nucleotide-binding domain (NBD1) of the cystic fibrosis transmembrane conductance regulator (CFTR). Here authors we develop nanobodies targeting NBD1 of human CFTR and demonstrate their ability to stabilize both isolated NBD1 and full-length protein.Maud SigoillotMarie OvertusMagdalena GrodeckaDaniel SchollAbel Garcia-PinoToon LaeremansLihua HeEls PardonEllen HildebrandtIna UrbatschJan SteyaertJohn R. RiordanCedric GovaertsNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Maud Sigoillot
Marie Overtus
Magdalena Grodecka
Daniel Scholl
Abel Garcia-Pino
Toon Laeremans
Lihua He
Els Pardon
Ellen Hildebrandt
Ina Urbatsch
Jan Steyaert
John R. Riordan
Cedric Govaerts
Domain-interface dynamics of CFTR revealed by stabilizing nanobodies
description The leading cause of cystic fibrosis is the deletion of phenylalanine 508 (F508del) in the first nucleotide-binding domain (NBD1) of the cystic fibrosis transmembrane conductance regulator (CFTR). Here authors we develop nanobodies targeting NBD1 of human CFTR and demonstrate their ability to stabilize both isolated NBD1 and full-length protein.
format article
author Maud Sigoillot
Marie Overtus
Magdalena Grodecka
Daniel Scholl
Abel Garcia-Pino
Toon Laeremans
Lihua He
Els Pardon
Ellen Hildebrandt
Ina Urbatsch
Jan Steyaert
John R. Riordan
Cedric Govaerts
author_facet Maud Sigoillot
Marie Overtus
Magdalena Grodecka
Daniel Scholl
Abel Garcia-Pino
Toon Laeremans
Lihua He
Els Pardon
Ellen Hildebrandt
Ina Urbatsch
Jan Steyaert
John R. Riordan
Cedric Govaerts
author_sort Maud Sigoillot
title Domain-interface dynamics of CFTR revealed by stabilizing nanobodies
title_short Domain-interface dynamics of CFTR revealed by stabilizing nanobodies
title_full Domain-interface dynamics of CFTR revealed by stabilizing nanobodies
title_fullStr Domain-interface dynamics of CFTR revealed by stabilizing nanobodies
title_full_unstemmed Domain-interface dynamics of CFTR revealed by stabilizing nanobodies
title_sort domain-interface dynamics of cftr revealed by stabilizing nanobodies
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/2a36a5cc137946bdbc014d5d58e302cb
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