Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites
Src is a prototypical signaling non-receptor protein tyrosine kinase that interconverts between distinct conformations. Here the authors use variants of the kinase-inhibitor dasatinib to define three specific conformational states of the Src kinase and shed insight on the effect of conformation-spec...
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2017-12-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-017-02240-6 |
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doaj-01dc8ef23c534552afe3e1801c1b9be52021-05-11T07:06:38ZengNature Publishing GroupNature Communications2041-17232017-12-018111510.1038/s41467-017-02240-6Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sitesMichael Tong0Jeff G. Pelton1Michelle L. Gill2Weibing Zhang3Francis Picart4Markus A. Seeliger5Department of Pharmacological Sciences, Stony Brook University Medical SchoolQB3 Institute, University of CaliforniaStructural Biophysics Laboratory, National Cancer InstituteDepartment of Pharmacological Sciences, Stony Brook University Medical SchoolDepartment of Chemistry, Stony Brook UniversityDepartment of Pharmacological Sciences, Stony Brook University Medical SchoolSrc is a prototypical signaling non-receptor protein tyrosine kinase that interconverts between distinct conformations. Here the authors use variants of the kinase-inhibitor dasatinib to define three specific conformational states of the Src kinase and shed insight on the effect of conformation-specific inhibitors on Src dynamics.https://doi.org/10.1038/s41467-017-02240-6 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Michael Tong Jeff G. Pelton Michelle L. Gill Weibing Zhang Francis Picart Markus A. Seeliger |
spellingShingle |
Michael Tong Jeff G. Pelton Michelle L. Gill Weibing Zhang Francis Picart Markus A. Seeliger Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites Nature Communications |
author_facet |
Michael Tong Jeff G. Pelton Michelle L. Gill Weibing Zhang Francis Picart Markus A. Seeliger |
author_sort |
Michael Tong |
title |
Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites |
title_short |
Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites |
title_full |
Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites |
title_fullStr |
Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites |
title_full_unstemmed |
Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites |
title_sort |
survey of solution dynamics in src kinase reveals allosteric cross talk between the ligand binding and regulatory sites |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2017-12-01 |
description |
Src is a prototypical signaling non-receptor protein tyrosine kinase that interconverts between distinct conformations. Here the authors use variants of the kinase-inhibitor dasatinib to define three specific conformational states of the Src kinase and shed insight on the effect of conformation-specific inhibitors on Src dynamics. |
url |
https://doi.org/10.1038/s41467-017-02240-6 |
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