Network approach of the conformational change of c-Src, a tyrosine kinase, by molecular dynamics simulation
- Authors
- Yoon, Hyun Jung; Lee, Sungmin; Park, Sun Joo; Wu, Sangwook
- Issue Date
- 4-4월-2018
- Publisher
- NATURE PUBLISHING GROUP
- Citation
- SCIENTIFIC REPORTS, v.8
- Indexed
- SCIE
SCOPUS
- Journal Title
- SCIENTIFIC REPORTS
- Volume
- 8
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/76166
- DOI
- 10.1038/s41598-018-23964-5
- ISSN
- 2045-2322
- Abstract
- Non-receptor tyrosine kinase c-Src plays a critical role in numerous cellular signalling pathways. Activation of c-Src from its inactive to the active state involves large-scale conformational changes, and is controlled by the phosphorylation state of two major phosphorylation sites, Tyr416 and Tyr527. A detailed mechanism for the entire conformational transition of c-Src via phosphorylation control of Tyr416 and Tyr527 is still elusive. In this study, we investigated the inactive-to-active conformational change of c-Src by targeted molecular dynamics simulation. Based on the simulation, we proposed a dynamical scenario for the activation process of c-Src. A detailed study of the conformational transition pathway based on network analysis suggests that Lys321 plays a key role in the c-Src activation process.
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