Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase

The Bcr-Abl tyrosine kinases p210 and p190 are linked to different leukemias and differ by the Dbl homology (DH) and Pleckstrin-homology (PH) domains. Here the authors characterize structures of the Bcr-Abl p210 DH and PH domains and find that the PH domain is important for the cellular localization...

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Autores principales: Sina Reckel, Charlotte Gehin, Delphine Tardivon, Sandrine Georgeon, Tim Kükenshöner, Frank Löhr, Akiko Koide, Lena Buchner, Alejandro Panjkovich, Aline Reynaud, Sara Pinho, Barbara Gerig, Dmitri Svergun, Florence Pojer, Peter Güntert, Volker Dötsch, Shohei Koide, Anne-Claude Gavin, Oliver Hantschel
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Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/dc5c32c8cdcb4768b619089187cee0d3
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spelling oai:doaj.org-article:dc5c32c8cdcb4768b619089187cee0d32021-12-02T14:41:59ZStructural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase10.1038/s41467-017-02313-62041-1723https://doaj.org/article/dc5c32c8cdcb4768b619089187cee0d32017-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02313-6https://doaj.org/toc/2041-1723The Bcr-Abl tyrosine kinases p210 and p190 are linked to different leukemias and differ by the Dbl homology (DH) and Pleckstrin-homology (PH) domains. Here the authors characterize structures of the Bcr-Abl p210 DH and PH domains and find that the PH domain is important for the cellular localization and signaling network of p210.Sina ReckelCharlotte GehinDelphine TardivonSandrine GeorgeonTim KükenshönerFrank LöhrAkiko KoideLena BuchnerAlejandro PanjkovichAline ReynaudSara PinhoBarbara GerigDmitri SvergunFlorence PojerPeter GüntertVolker DötschShohei KoideAnne-Claude GavinOliver HantschelNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Sina Reckel
Charlotte Gehin
Delphine Tardivon
Sandrine Georgeon
Tim Kükenshöner
Frank Löhr
Akiko Koide
Lena Buchner
Alejandro Panjkovich
Aline Reynaud
Sara Pinho
Barbara Gerig
Dmitri Svergun
Florence Pojer
Peter Güntert
Volker Dötsch
Shohei Koide
Anne-Claude Gavin
Oliver Hantschel
Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase
description The Bcr-Abl tyrosine kinases p210 and p190 are linked to different leukemias and differ by the Dbl homology (DH) and Pleckstrin-homology (PH) domains. Here the authors characterize structures of the Bcr-Abl p210 DH and PH domains and find that the PH domain is important for the cellular localization and signaling network of p210.
format article
author Sina Reckel
Charlotte Gehin
Delphine Tardivon
Sandrine Georgeon
Tim Kükenshöner
Frank Löhr
Akiko Koide
Lena Buchner
Alejandro Panjkovich
Aline Reynaud
Sara Pinho
Barbara Gerig
Dmitri Svergun
Florence Pojer
Peter Güntert
Volker Dötsch
Shohei Koide
Anne-Claude Gavin
Oliver Hantschel
author_facet Sina Reckel
Charlotte Gehin
Delphine Tardivon
Sandrine Georgeon
Tim Kükenshöner
Frank Löhr
Akiko Koide
Lena Buchner
Alejandro Panjkovich
Aline Reynaud
Sara Pinho
Barbara Gerig
Dmitri Svergun
Florence Pojer
Peter Güntert
Volker Dötsch
Shohei Koide
Anne-Claude Gavin
Oliver Hantschel
author_sort Sina Reckel
title Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase
title_short Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase
title_full Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase
title_fullStr Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase
title_full_unstemmed Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase
title_sort structural and functional dissection of the dh and ph domains of oncogenic bcr-abl tyrosine kinase
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/dc5c32c8cdcb4768b619089187cee0d3
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