Primary insights into structure and structururally determined features of C2 domain of Bcr

DomAIn oF BcrThe investigation of the C2 domain of Bcr is critical for understanding the functions of normal Bcr protein and the processes in cancer involving the hybrid Bcr-Abl.Aim: This study aimed to estimate the structure and lipid-binding capacity of the C2 domain of Bcr.Methods: The secondary and tertiary structures were predicted using various bioinformatic tools.A DNA fragment encoding the C2 domain was introduced into the expression vector pET28 using sequence and ligation-independent cloning techniques.The purified recombinant C2 domain was used to obtain circular dichroism spectra and perform a lipid-binding assay.Results: The structure predictions indicate that the C2 domain of Bcr likely adopts a typical beta-sandwich structure with type II topology.The circular dichroism data on the purified recombinant C2 domain confirmed the expected predominance of beta-structures.Binding to eight phospholipids was identified.Conclusions: The recombinant C2 domain of Bcr has a structure comparable to other well-studied C2 domains.Binding to various lipids suggests a possible specific localization of the Bcr protein on different cellular membrane structures.