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https://doi.org/10.3938/NPSM.69.984
A Study on Imatinib Binding to c-Src Tyrosine Kinase According to Sequential Conformational Change
New Phys.: Sae Mulli 2019; 69: 984~988
Published online September 30, 2019;  https://doi.org/10.3938/NPSM.69.984
© 2019 New Physics: Sae Mulli.

Suhyun PARK1, Sangwook WU2,3*

1Department of Physics, Pukyong National University, Busan 48513, Korea
2Department of Physics, Pukyong National University, Busan 48513, Korea
3PharmCADD, Busan 48059, Korea
Correspondence to: sangwoow@pknu.ac.kr
Received August 13, 2019; Revised August 26, 2019; Accepted August 26, 2019.
cc This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract

c-Src tyrosine kinase plays a key role in cell differentiation and growth. Imatinib (Gleevec^{\circledR}) is an effective inhibitor for suppressing the activity of Abl-tyrosine kinase. c-Src tyrosine kinase has a 47 percent similarity to Abl tyrosine kinase in the amino acid sequence.

We investigate the binding of imatinib to c-Src tyrosine kinase by using MD simulation and molecular docking. In particular, we use a targeted MD simulation to generate several conformational structures in the process of the conformational change of c-Src tyrosine kinase from an inactive state to an active state. The results establish that most stable conformation of c-Src tyrosine kinase to imatinib, from among the various conformations, has the highest binding affinity

PACS numbers: 87.15.He, 87.14.Ee
Keywords: Allosteric protein, MD simulation, Docking


October 2019, 69 (10)
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