人白细胞分化抗原19蛋白结构与功能的生物信息学分析

Bioinformatics analysis of structure and function of cluster of differentiation 19

目的运用生物信息学方法对人白细胞分化抗原19(B-lymphocyte antigen CD19,以下简称CD19)蛋白的理化性质、空间结构、蛋白质的修饰位点以及相互作用网络进行分析。方法从蛋白质数据库(Universal Protein, UniProt)获取人CD19蛋白的序列信息,并运用ExPASy、SignalP 5.0 Server、TMHMMServer v.2.0、SOPMA、SWISS-MODEL、UniProt数据库、STRING、Pymol等对人CD19蛋白进行全面、系统的分析。结果软件预测及已经解析的结构显示,人CD19蛋白由信号肽、胞外域、跨膜域及胞内域组成,其胞外域结构主要由β折叠片组成,跨膜域由一段α螺旋组成,已报道的磷酸化位点有6个,N糖基化位点有5个。与人CD19蛋白形成蛋白网络的蛋白有10个,分别是CD79A、CR2、LYN、CD79B、CD81、SYK、VAV1、BTK、BCL6和IGLL5。人CD19蛋白参与的信号通路有B细胞受体信号通路、Fc epsilon RI信号通路等,此外,还参与原发性免疫缺陷以及EB病毒感染等。结论经过软件分析及结构预测分析,阐述了人CD19蛋白的结构与功能的关系,为免疫治疗药物的开发提供参考依据。

Objective To analyze the physicochemical properties, three-dimensional structure, protein modification sites and interaction network of B-lymphocyte antigen CD19 by bioinformatics methods. Methods Sequence information of human CD19 protein was obtained from the Universal Protein Database(UniProt). Systematic analysis of the CD19 protein was performed by using the software of ExPASy, SignalP 5.0 Server, TMHMMServer v.2.0, SOPMA, SWISS-MODEL, Uniprot database, STRING and Pymol. Results The structure prediction and analysis of CD19 showed that it is a transmembrane protein, consisting of a signal peptide, an extracellular domain, a transmembrane domain and an intracellular domain. The extracellular domain structure was mainly composed of beta pleated sheet, and the transmembrane domain was composed of an alpha helix. There were six reported phosphorylation sites and five N-linked glycosylation sites. There were 10 proteins(CD79 A, CR2, LYN, CD79 B, CD81, SYK, VAV1, BTK, BCL6, and IGLL5) that form a protein network with CD19. CD19 was involved in B cell receptor signaling pathway, Fc epsilon RI signaling pathway, primary immunodeficiency and Epstein-Barr virus infection. Conclusion The relationship between structure and function of CD19 protein was investigated by structure analysis and prediction, which could provide a basis for the development of targeted drugs.