期刊论文

Analysis of the molecular structure and physicochemical property of human Ryanodine receptors

中文

生物学杂志

2095-1736

2019

36

5

25-30

10.3969/j.issn.2095-1736.2019.05.025

81673227:国家自然科学基金 81172712:国家自然科学基金 2018KYY220:南华大学研究生科学基金项目

本校为第一机构

Ryanodine受体(Ryanodine receptor,RyR)是一种重要的配体门控的Ca~(2+)通道,分析RyR蛋白的结构及其理化性质对了解其调控机制具有重要意义。运用生物信息学方法,对RyR 3种亚型蛋白进行了分子结构和理化性质分析。结果显示RyR 3种亚型均具有跨膜结构,为亲水性蛋白,具有磷酸化位点,含有大量α-螺旋,无二硫键,有蛋白结合能力和离子通道活性等,参与离子转运等。对RyR蛋白进行分子结构和理化性质等生物信息学分析,为RyR的机制研究及生物学实验等提供重要的参考依据。

Ryanodine receptor (RyR) is an important ligand-gated Ca 2+ channel. It is of great significance to analyze the structure and physicochemical properties of RyR, so that we can understand its regulation mechanism. In this study, bioinformatics methods were used to analyze the three subtypes of RyR (RyRs). The results showed that RyRs were hydrophilic protein, which have transmembrane structure, phosphorylation sites, and a large number of α-helix, but no disulfide bonds. RyRs have protein bonding and ion channel activity, participate in ion tra...