Abstract: Objective To study the effect of platelet CD36 antigen deletion type I gene mutation on its protein structure and function, and to understand the relationship between CD36 antigen deletion type I gene mutation and protein structure and function. Methods The DNA of platelet CD36 antigen deletion type I was amplified by PCR and sequenced. The obtained DNA sequence was aligned with the wild-type sequence of the CD36 gene, the start and end points of 12 exons were confirmed, and the cDNA sequence of exon 2 to 14 was spliced. Missense and synonymous mutations in cDNA sequences were analyzed with MEGA5.04 software. Psipred, SOPMA and JPred4 were used to predict the secondary structure of the protein, SWISS-MODEL to predict the spatial structure of the amino acid chain, Mupro, SDM, CUPSAT, mSCM, DUET, Dynamut to predict the stability change of the protein before and after mutation, PROVEAN to predict the effect on protein function, PyMOL and LigPlot+ modified protein spatial structure prediction map. Results A total of 4 gene mutations E4 (275). E12 (1156). E14 (1409) C>T and E6(538) T>C base mutations were detected. All 4 mutations lead to changes in protein structure and reduced stability. 3 kinds of c.T92M, c.W180R, c.R386W mutations have adverse effects on the function, the 5LGD model and the interaction between the mutant protein's ligand receptor basically unchanged. Conclusion CD36 antigen deletion type I base mutation reduces the protein stability by changing the protein structure, among which c.T92M, c.W180R, c.R386W mutations have a negative impact on protein function.

Key words: CD36, Gene mutation, Enzyme protein structure, Protein stability, Bioinformation