Fig. 4. Protein-ligand docking study of sesquiterpene lactones in STAT3. (A) Domain structured of STAT3. SH2, Src homology 2; TAD, transactivation domain. (B) X-ray crystal structure of p-STAT3 homodimer. (C) Key interacting amino acid residues of pTyr705 in SH2 domain binding pocket. Hydrogen bonds were shown in black dashes. (D) The location of SH2 domain binding pocket. Selected docking poses of sesquiterpene lactones; (E) alantolactone, (F) isoalantolactone, (G) parthenolide, (H) costunolide, (I) atractylenoide I, and (J) sclareolide. Top ten most energy-minimized binding modes of (K) dehydrocostus lactone, and (L) tulipalin A were compared with those of alantolactone.
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