Abstract: AIM: To analyze the binding area of atractyloside targeting oncoprotein BORIS to inhibit cancer cell proliferation.  METHODS: DNAMAN comparison sequences were used to find the conserved regions of BORIS. Conservative regions were elected and the structure were predicted using SWISS-MODEL. ChemBio3D Ultra was used for minimum structure quantification, and Autodocking for molecular docking. The BORIS of the corresponding segment were overexpressed for verification. RESULTS: BORIS-N end had relatively conserved regions and high-level structures in the biological evolution process. The N-terminal of human-derived BORIS was the main action area we speculated, especially the 70th to 97th amino acids, and the site that binded preferentially to atractyloside after molecular docking was the 96th position (Glutamine), and this area would inhibit cell proliferation. CONCLUSION: BORIS-N terminal and atractyloside have an action area, and this segment has an important effect on cell proliferation, which is of great significance for the future screening of targeted drugs.

Key words: atractyloside, BORIS,  protein structure, molecular interaction, molecular targeted therapy