Interactions between delphinidin-3-O-arabinoside and a homodimer of the dimerization domain of hepatocyte nuclear factor-1α (HNF-1α).
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The conformation of delphinidin-3-O-arabinoside with the highest binding affinity for the dimerization domain of HNF-1α as a homodimer is shown (A) with a lilac surface representing a general surface of the homodimer (A, C). Amino acids in the homodimer of the dimerization domain of HNF-1α had electrostatic (pink) and van der Waals (green) interactions with delphinidin-3-O-arabinoside (B). A hydrogen bond between atoms in the main-chain of SER6 and delphinidin-3-O-arabinoside is represented by a one headed, dashed green arrow. A 3-dimensional representation of delphinidin-3-O-arabinoside interacting with the dimerization domain of HNF-1α as a homodimer is shown (C) with certain interacting amino acids highlighted and labeled to show their relative position.