α-1,6-岩藻糖基转移酶的生物信息学分析

Bioinformatics Analysis ofα-1,6-fucosyltransferase

核心岩藻糖糖基化作为一种较常见N-糖基化,是重要的翻译后修饰机制,可以快速改变蛋白质的生物学性质,在哺乳动物细胞识别、增殖以及代谢活动中具有重要的作用。在人类,α-1,6-岩藻糖基转移酶(FUT8)是此修饰过程的唯一蛋白。利用生物信息学分析FUT8蛋白的编码基因结构、蛋白质的氨基酸序列特征和三维结构的信息,解析其生物学功能。利用NCBI网站生物信息数据库及在线工具分析fut8基因的结构及表达调控特点;分析FUT8蛋白的理化性质、跨膜结构域、立体结构、蛋白相互作用网络及通路,明确其生物功能及其在相关疾病中的作用。编码FUT8的人类fut8基因位于14q23.3,转录产物最长3895 bp,共编码氨基酸575个,产物FUT8为弱碱亲水性,存在由内向外的跨膜区段,二级结构元件以α螺旋为主,可分为4个结构域,与多种蛋白质及受体存在相互作用,催化蛋白质核心岩藻糖基化的形成,序列比对表明FUT8存在多个保守域并在物种进化中高度保守。利用生物信息数据库及工具成功获取人FUT8蛋白的理化性质、跨膜域信息、立体结构,以及其与多种蛋白的相互作用网络,为未来进一步研究FUT8在肥胖及相关疾病、肿瘤转移炎症及免疫和造血异常中的作用提供理论依据。

As a common N-glycosylation,core fucosylation is an important post-translational modification mechanism,which can quickly change the biological properties of proteins and the activity of enzyme.Core fucosylation plays an important role in mammalian cell recognize,proliferate and metabolism.In human beings,α-1,6-Fucosyltransferase(FUT8)is the only protein which possesses core fucosyltransferase activity.In order to analyze the structure and expression of fut8 gene coding FUT8 protein,amino acid sequence,three-dimensional structure information and the protein interaction networks of FUT8 protein were analyzed by using bioinformatics to explore its functions and its role in related disease.The structure,location,and expression regulation characteristics of fut8 gene were analyzed by using GenBank database of NCBI website.The physical and chemical properties,transmembrane domain,three-dimensional structure,protein interaction networks and pathways of FUT8 protein were analyzed by GenPept and PDB databases,and ProtParam,PPI and KEGG tools etc.The human fut8 gene is located at 14q23.3 while the longest transcription product is 3895 bp,encoding a protein with 575 amino acids.The product protein,FUT8,is weakly alkaline and hydrophilic,with a transmembrane segment from the inside to the outside.The main element of FUT8 secondary structure is alpha helix,which forms 4 domains.FUT8 interacts with a variety of proteins and receptors,catalyzes the formation of core fucosylation of the protein.Sequence alignment shows that FUT8 has multiple conserved domains and is highly conserved in species evolution.The physicochemical properties,theoretical transmembrane domain information,three-dimensional structure,protein pathways and interaction networks of human FUT8 protein have been successfully obtained by multiple bioinformatics databases and tools,which provide theoretical basis for further study of FUT8 in the fields of obesity and related diseases,tumor metastasis,inflammation,dysimmunity and hematopoiesis abnormal.