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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Main Authors: Michael Tong, Jeff G. Pelton, Michelle L. Gill, Weibing Zhang, Francis Picart, Markus A. Seeliger
Format: Article
Language:English
Published: Nature Publishing Group 2017-12-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-02240-6
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spelling 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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