Dynamic conformational characteristics of the R102Q mutant of neuronal calcium sensor-1 protein
10.3969/j.issn.2095-4344.2015.02.012
- VernacularTitle:神经元钙传感蛋白R102Q突变体的动力学构象特征
- Author:
Yuzhen ZHU
;
Qingwen ZHANG
- Publication Type:Journal Article
- Keywords:
Neuronal Calcium-Sensor Proteins;
Amino Acids;
Mutation;
Neurons
- From:
Chinese Journal of Tissue Engineering Research
2015;(2):225-230
- CountryChina
- Language:Chinese
-
Abstract:
BACKGROUND:Neuronal calcium sensor-1 protein has a variety of different neuronal functions and has a high distribution in different areas of the brain. A single residue R102Q mutation in human neuronal calcium sensor-1 protein is demonstrated to be associated with autism disease. The experiment studies have reported that this R102Q mutant has essential conformation changes in local area of the neuronal calcium sensor-1. OBJECTIVE: To wel understand the specific reasons of the R102Q mutation of the neuronal calcium sensor-1 to the conformational dynamic changes. METHODS:Six independent extensive al-atom molecule dynamic simulations during 0-450 ns were conducted. RESULTS AND CONCLUSION: We have found that (1) there is no obvious recombination during the simulations between wild type and mutant type, but R102Q mutant alters the helix and makes the structure of the protein more stable; (2) R102Q mutation alters the salt bridges, reduces the flexibility of L2, and makes L3 extend in hydrophobic crevice. These results reveal that the helix plays an important role in the structural stability, and salt bridge is the important reason for the dynamic changes of neuronal calcium sensor-1 protein. This study may provide a structural insight into the function of protein deficiency associated with R102Q mutant.
