论文部分内容阅读
目的应用生物信息学技术预测曼氏血吸虫己糖激酶(SmHK)的结构和功能,为进一步功能研究提供信息。方法从GenBank获取SmHK及其他物种HK全长cDNA序列及氨基酸序列,应用NCBI、Expasy等在线生物信息学网站及VectorNTI软件包,对所获氨基酸序列的保守功能域及基序、蛋白质理化参数、亚细胞定位、亲水性、B细胞线性表位、二级结构及拓扑结构、三级结构建模分析及预测。结果SmHK编码451氨基酸残基,理论分子量为50446.01Da,具有完整HK-1及HK-2保守功能域,与结构和功能有关的位点高度保守,与宿主(人、鼠)的同源性为30%,与人等脊椎动物有较近的进化关系;有多个潜在的抗原表位、多个磷酸化位点及1个跨膜结构。三级结构分子建模显示该蛋白两基团间有一裂隙,葡萄糖、ATP结合位点及ATP催化区位于该裂隙中或周围,跨膜区与其两端的碱性氨基酸形成一阴离子通道。结论SmHK与结构和功能相关的位点高度保守,与宿主有较近的进化关系,推测该蛋白可能通过跨膜区锚定在线粒体外膜上,主要功能位点位于蛋白裂隙中或周围,多个磷酸化位点说明其参与多种细胞功能的调节,在调节能量代谢中起重要作用,是潜在的疫苗候选分子和药物作用靶标。
Objective To predict the structure and function of Schistosoma mansoni hexokinase (SmHK) using bioinformatics techniques and provide information for further functional studies. Methods The full-length cDNA sequence and amino acid sequence of SmHK and other species were obtained from GenBank. The conserved domains and motifs of amino acid sequence, protein physicochemical parameters, Cell localization, hydrophilicity, B cell linear epitope, secondary structure and topology, tertiary structure modeling and prediction. RESULTS: SmHK encoded a 451 amino acid residue with a theoretical molecular mass of 50446.01 Da. It had a complete conserved domain of HK-1 and HK-2 and highly conserved structural and functional sites. The homology with the host (human and mouse) was 30%, and humans and other vertebrates have a closer evolutionary relationship; there are several potential epitopes, multiple phosphorylation sites and a transmembrane structure. Molecular modeling of the tertiary structure showed that there was a gap between the two groups of the protein. Glucose, ATP binding sites and ATP catalytic region were located in or around the fracture, and an anion channel was formed between the transmembrane domain and the basic amino acids at both ends. Conclusion SmHK is highly conserved in its structure and function and has a close evolutionary relationship with the host. It is speculated that the SmHK may be anchored to the mitochondrial outer membrane through the transmembrane region, with major functional sites located in or around the protein fissures Phosphorylation sites indicate that they are involved in the regulation of various cellular functions and play an important role in the regulation of energy metabolism and are potential vaccine candidate molecules and drug targets.