Structural and functional consequences of the STAT5BN642H driver mutation
Hyper-activated STAT5B and its disease-causing variants are of interest as cancer drug targets. Here the authors combine cell based studies, X-ray crystallography, biophysical experiments and MD simulations to structurally and functionally characterize the STAT5BN642H mutant found in aggressive T-ce...
Main Authors: | , , , , , , , , , , , , , , , , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2019-06-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-019-10422-7 |
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author | Elvin D. de Araujo Fettah Erdogan Heidi A. Neubauer Deniz Meneksedag-Erol Pimyupa Manaswiyoungkul Mohammad S. Eram Hyuk-Soo Seo Abdul K. Qadree Johan Israelian Anna Orlova Tobias Suske Ha T. T. Pham Auke Boersma Simone Tangermann Lukas Kenner Thomas Rülicke Aiping Dong Manimekalai Ravichandran Peter J. Brown Gerald F. Audette Sarah Rauscher Sirano Dhe-Paganon Richard Moriggl Patrick T. Gunning |
author_facet | Elvin D. de Araujo Fettah Erdogan Heidi A. Neubauer Deniz Meneksedag-Erol Pimyupa Manaswiyoungkul Mohammad S. Eram Hyuk-Soo Seo Abdul K. Qadree Johan Israelian Anna Orlova Tobias Suske Ha T. T. Pham Auke Boersma Simone Tangermann Lukas Kenner Thomas Rülicke Aiping Dong Manimekalai Ravichandran Peter J. Brown Gerald F. Audette Sarah Rauscher Sirano Dhe-Paganon Richard Moriggl Patrick T. Gunning |
author_sort | Elvin D. de Araujo |
collection | DOAJ |
description | Hyper-activated STAT5B and its disease-causing variants are of interest as cancer drug targets. Here the authors combine cell based studies, X-ray crystallography, biophysical experiments and MD simulations to structurally and functionally characterize the STAT5BN642H mutant found in aggressive T-cell leukemia and lymphomas and find that it has an increased affinity for self-dimerization. |
first_indexed | 2024-12-17T19:28:39Z |
format | Article |
id | doaj.art-f8b672c48f8f4b91911646f53ce84f0b |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-17T19:28:39Z |
publishDate | 2019-06-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-f8b672c48f8f4b91911646f53ce84f0b2022-12-21T21:35:19ZengNature PortfolioNature Communications2041-17232019-06-0110111510.1038/s41467-019-10422-7Structural and functional consequences of the STAT5BN642H driver mutationElvin D. de Araujo0Fettah Erdogan1Heidi A. Neubauer2Deniz Meneksedag-Erol3Pimyupa Manaswiyoungkul4Mohammad S. Eram5Hyuk-Soo Seo6Abdul K. Qadree7Johan Israelian8Anna Orlova9Tobias Suske10Ha T. T. Pham11Auke Boersma12Simone Tangermann13Lukas Kenner14Thomas Rülicke15Aiping Dong16Manimekalai Ravichandran17Peter J. Brown18Gerald F. Audette19Sarah Rauscher20Sirano Dhe-Paganon21Richard Moriggl22Patrick T. Gunning23Department of Chemical and Physical Sciences, University of Toronto MississaugaDepartment of Chemical and Physical Sciences, University of Toronto MississaugaInstitute of Animal Breeding and Genetics, University of Veterinary Medicine ViennaDepartment of Chemical and Physical Sciences, University of Toronto MississaugaDepartment of Chemical and Physical Sciences, University of Toronto MississaugaDalriada Drug Discovery, University of Toronto MississaugaDepartment of Cancer Biology, Dana-Farber Cancer InstituteDepartment of Chemical and Physical Sciences, University of Toronto MississaugaDepartment of Chemical and Physical Sciences, University of Toronto MississaugaInstitute of Animal Breeding and Genetics, University of Veterinary Medicine ViennaInstitute of Animal Breeding and Genetics, University of Veterinary Medicine ViennaInstitute of Animal Breeding and Genetics, University of Veterinary Medicine ViennaInstitute of Laboratory Animal Science, University of Veterinary Medicine ViennaUnit of Laboratory Animal Pathology, University of Veterinary Medicine ViennaLudwig Boltzmann Institute for Cancer ResearchInstitute of Laboratory Animal Science, University of Veterinary Medicine ViennaStructural Genomics Consortium, University of TorontoStructural Genomics Consortium, University of TorontoStructural Genomics Consortium, University of TorontoDepartment of Chemistry, York UniversityDepartment of Chemical and Physical Sciences, University of Toronto MississaugaDepartment of Cancer Biology, Dana-Farber Cancer InstituteInstitute of Animal Breeding and Genetics, University of Veterinary Medicine ViennaDepartment of Chemical and Physical Sciences, University of Toronto MississaugaHyper-activated STAT5B and its disease-causing variants are of interest as cancer drug targets. Here the authors combine cell based studies, X-ray crystallography, biophysical experiments and MD simulations to structurally and functionally characterize the STAT5BN642H mutant found in aggressive T-cell leukemia and lymphomas and find that it has an increased affinity for self-dimerization.https://doi.org/10.1038/s41467-019-10422-7 |
spellingShingle | Elvin D. de Araujo Fettah Erdogan Heidi A. Neubauer Deniz Meneksedag-Erol Pimyupa Manaswiyoungkul Mohammad S. Eram Hyuk-Soo Seo Abdul K. Qadree Johan Israelian Anna Orlova Tobias Suske Ha T. T. Pham Auke Boersma Simone Tangermann Lukas Kenner Thomas Rülicke Aiping Dong Manimekalai Ravichandran Peter J. Brown Gerald F. Audette Sarah Rauscher Sirano Dhe-Paganon Richard Moriggl Patrick T. Gunning Structural and functional consequences of the STAT5BN642H driver mutation Nature Communications |
title | Structural and functional consequences of the STAT5BN642H driver mutation |
title_full | Structural and functional consequences of the STAT5BN642H driver mutation |
title_fullStr | Structural and functional consequences of the STAT5BN642H driver mutation |
title_full_unstemmed | Structural and functional consequences of the STAT5BN642H driver mutation |
title_short | Structural and functional consequences of the STAT5BN642H driver mutation |
title_sort | structural and functional consequences of the stat5bn642h driver mutation |
url | https://doi.org/10.1038/s41467-019-10422-7 |
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