人髓样分化因子88（MyD88）属于Toll样受体和IL1受体家族成员下游的炎症信号通路的中心因子。为了研究人MyD88的蛋白结构和功能，本文利用重要数据库进行了生物信息学分析。研究表明，人MyD88基因全长为5 670 bp，位于染色体3p22.2，共编码296个氨基酸。人MyD88蛋白具有较高的保守性，其等电点为5.64，不存在信号肽，并且含有2个苏木化位点、15个丝氨酸磷酸化位点、6个苏氨酸磷酸化位点和4个酪氨酸磷酸化位点。该蛋白主要定位在细胞核和细胞质中，而且在血液、脾脏和肺较多，其二级结构含有145个α螺旋和30个β折叠，拉曼图表明三级结构模型A是可信的。与人MyD88相互作用的蛋白主要是Toll样受体和白介素相关蛋白，并且参与炎症反应、细胞凋亡等重要的免疫过程。本研究为阐明人MyD88基因结构特点和生物学功能奠定了理论基础，也为其相关疾病诊断和治疗提供了新思路。

Human myeloid differentiation factor 88 (MyD88) is the central factor for inflammatory signaling pathways downstream of members of the Tolllike receptor (TLR) and interleukin1 (IL1) receptor families. To explore the human MyD88 structures and functions by bioinformatics analysis, results showed human MyD88 gene of full length 5 670 bp, located on chromosome 3p22.2， and encoded 296 amino acids, which was a higher conserved one. Meanwhile, human MyD88 was highly distributed in the blood, spleen and lung, with no signal peptides, whereas it included 2 sumolation sites and 15 serine phosphorylation sites, 6 threonine phosphorylation sites and 4 tyrosine phosphorylation sites. The secondary structure was mainly consisted of 145 αhelix and 30 βsheet regions, indicating that the tertiary structure was reliable by ramachandran plot. In addition, human MyD88 also has protein interaction with Tolllike receptors and interleukins, participating in inflammatory reaction, cell apoptosis and other immunologic processes. All together, our bioinformatics analysis would provide a basis for understanding structure features and biological functions of human MyD88, guiding a new schema for the diagnosis and treatment in the future.