Neuritin结构组成分析及其相互作用蛋白生物信息学预测  

Structural composition analysis of Neuritin and bioinformatics prediction of its interactive proteins

作　　者：李煜 孟平平 王宿洁 朱礼彦 朱金辉 陈仁伟 杨磊[2] LI Yu;MENG Pingping;WANG Sujie;ZHU Liyan;ZHU Jinhui;CHEN Renwei;YANG Lei(School of Medicine,Shihezi University,Shihezi,Xinjiang 832000,China;Department of Medicine,Hangzhou Normal University,Hangzhou,Zhejiang 310036,China)

机构地区：[1]石河子大学医学院,新疆石河子832000 [2]杭州师范大学医学院,浙江杭州310036

出　　处：《石河子大学学报（自然科学版）》2023年第1期87-92,共6页Journal of Shihezi University(Natural Science)

基　　金：国家科技重大专项(民口)重大新药创制项目(2019ZX09301-161);浙江省重点研发项目(2019C03060)。

摘　　要：目的对Neuritin的理化性质及结构组成,蛋白质相互作用网络进行生物信息学预测分析,为进一步研究Neuritin的功能和作用机制提供新的思路与方向。方法应用Protscale和ProtParam、TMHMM、SignalP、PSORTⅡ、NetNGlyc、NetOGlyc和Netphos等软件,分析Neuritin的理化性质、跨膜结构、信号肽结构、亚细胞定位以及翻译后修饰位点;利用Protean、tFold以及AlaphFold等软件和数据库,分析Neuritin的二级和三级结构;同时,利用STRING数据库构建Neuritin蛋白质相互作用网络。结果Neuritin的相对分子质量为15332.77,理论等电点(PI)为6.54。不稳定系数27.26,属于较稳定蛋白;脂肪系数98.31;总平均亲水性0.208,属于疏水性蛋白;Neuritin表达产物N端27个氨基酸为信号肽,C端27个氨基酸为GPI锚定序列,为跨膜区;其亚细胞定位及可能性分别为胞外(34.8%)、细胞膜(34.8%)、内质网(17.4%)及高尔基体(13.0%);无N糖基化及O糖基化位点,存在11个磷酸化位点;由5段α-螺旋构成其主体结构;相互作用蛋白网络包括离子型谷氨酸受体AMPA(Gria)家族、嗅觉介导素(Olfm)家族等10个蛋白。结论Neuritin为经典的分泌蛋白,具有多个磷酸化氨基酸残基的潜在位点,整体呈现疏水性质,可能通过Gria蛋白家族发挥兴奋性突触传递作用,通过Cacng2蛋白调控胞内钙通路产生生物学效应,本研究为进一步探讨Neuritin的功能及发挥作用的机制提供了依据。Objective To predict and analyze the physical and chemical properties,structural composition and protein-protein interaction network of Neuritin by bioinformatics,so as to provide new ideas and directions for the further study of the function and mechanism of Neuritin.Methods The physicochemical properties,transmembrane structure,signal peptide structure,subcellular localization and post-translational modification sites of Neuritin were analyzed by using Protscale and Protparam,TMHMM,Signalp,PSORT Ⅱ,NetNGlyc,NetOGlyc and Netphos software.Analyze the secondary and tertiary structure of Neuritin by using Protean,tFold,AlaphFold and other software and databases;Meanwhile,the Neuritin protein interaction network was constructed by using string database.Results The relative molecular weight of Neuritin was 15332.77,and the theoretical isoelectric point(PI)was 6.54.The instability coefficient is 27.26,which belongs to a relatively stable protein.The fat coefficient is 98.31.The total average hydrophilicity is 0.208,which belongs to hydrophobic protein.The N-terminal 27 amino acids of Neuritin expression product are signal peptides,and the C-terminal 27 amino acids are GPI anchored sequences,which are transmembrane regions.The subcellular localization and possibility were extracellular(34.8%),cell membrane(34.8%),endoplasmic reticulum(17.4%)and Golgi apparatus(13.0%).There were 11 potential phosphorylation sites of amino acid residues without N-glycosylation and O-glycosylation sites.By five α-paragraphs the spiral forms its main structure.The interacting protein network includes 10 proteins such as glutamate AMPA ion channel receptor(Gria)family and olfactory mediators(Olfm)family.Conclusion Neuritin is a classic secretory protein with multiple phosphorylation sites and hydrophobic properties.It may play the role of excitatory synaptic transmission through Gria protein family and regulate the intracellular calcium pathway through Cacng2 protein to produce biological effects.This study provides a basis for further ex

关 键 词：NEURITIN 理化性质 结构预测 蛋白质相互作用网络 生物信息学 

分 类 号：R34[医药卫生—基础医学]