Fig. 6

Structural Insights into the Molecular Docking of Gyp LI with HSP90AA1, SRC, and CASP3. Molecular docking analyses elucidated the binding configurations, with the green rod structures representing Gyp LI and the pink fan structures delineating the respective binding sites. (A) The interaction between HSP90AA1 and Gyp LI was found to involve the residues GLU-200, LYS-204, and SER-211. (B) The binding of Gyp LI to SRC was characterized by interactions with the residues GLN-144, PHE-150, LYS-152, and THR-247. (C) The residues implicated in the binding of CASP3 to Gyp LI were identified as TYR-204, ASP-253, and TYR-501. (D) The immunohistochemical analysis revealed significantly elevated expression levels of HSP90AA1, SRC, and CASP3 in thyroid cancer tissues compared to normal thyroid tissues, suggesting their potential relevance in the pathophysiology of ATC