Abstract
To analyze the interaction between PML protein and TAB1 protein using bioinformatic approaches and experimentally verify the results. Using Rosetta software, a 3D model of TAB1 protein was constructed through a comparative modeling approach; the secondary structure of PML protein was retrieved in the PDB database and its crystal structure and 3D structure were resolved. Zdock 3.0.2 software was used to perform protein-protein docking of PML and TAB1, and the best conformation was extracted for molecular structure analysis of the docking model. The interaction between the two proteins was detected using immunoprecipitation in α-MMC-treated M1 inflammatory macrophages. When 6IMQ of PML was used as the docking site, PML protein formed 3 salt bridges, 6 hydrogen bonds and 6 hydrophobic interactions with TAB1 proteins; when 5YUF of PML was used as the docking site, PML protein formed 1 hydrogen bond, 3 electrostatic interactions and 9 hydrophobic interactions with TAB1 proteins, and both of the docking modes formed good molecular docking and interactions. In the M1 inflammatory macrophages treated with α-MMC for 4 h, positive protein bands of PML and TAB1 were detected in the cell lysates in PML-IP group. PML protein can interact strongly with TAB1 protein.
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Schedule a callMore From: Nan fang yi ke da xue xue bao = Journal of Southern Medical University
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