Molecular dynamics simulations to understand LRKK2 mutations in Parkinson |
| |
| Authors: | Yun-Bao Guo Jing Chen Xing-Dong Zhang Song-Bai Xu |
| |
| Affiliation: | 1. Department of Neurosurgery, The First Hospital of Jilin University, Changchun130021, P.R. China;2. Department of Orthopedics, China-Japan Union Hospital of Jilin University, Changchun130033, P.R. China;3. Department of Anatomy, College of Basic Medical Sciences, Jilin University, No. 126 Xinmin Street, Changchum, Jilin130021, P.R. China |
| |
| Abstract: | Mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common cause of Parkinson's disease (PD). LRRK2 contains a Ras of complex proteins (ROC) domain that may acts as a GTPase to regulate its protein kinase activity. Here, we performed 10 ns molecular dynamics simulations on LRRK2 Apo, complex with GDP and mutations (R1441C, R1441G and R1441H). Our results strongly suggest that the formations of helix in L1 and its pliable plays a major role in the LRRK2 functions. |
| |
| Keywords: | molecular dynamics simualtions LRRK2 mutation analysis Gromacs |
|
|
