Abstract:Abstract: Through the bioinformatics software for predictive analysis, human alpha-1 antitrypsin (A1AT) protein was found to be an exocrine protein composed of 418 amino acids, with an isoelectric point of 5.37. Homology analysis showed that there are two important functional regions located in the residues 73~93 and 351~372. Secondary structure of the protein was predicted to have 13 larger alpha-helical regions, accounting for 42.58% of the total protein. Advanced structural analysis revealed that the presence of the RCL domain had an important effect on the structure and function of the A1AT. GO and KEGG pathway analysis showed that A1AT takes part in anti-inflammatory response, blood coagulation and cell migration, invasion and proliferation. The bioinformatic analysis of the A1AT protein provides important theoretical data for its research in disease diagnosis and treatment.
引用本文:
杨 毅, 王兆松, 牛瑞芳. 人A1AT蛋白的生物信息学分析[J]. 生命科学研究, 2018, 22(1): 42-50.
YANG Yi, WANG Zhao-song, NIU Rui-fang. Bioinformatic Analysis of Human A1AT Protein. Life Science Research, 2018, 22(1): 42-50.