Interactions between delphinidin-3-<i>O</i>-arabinoside and a homodimer of the dimerization domain of hepatocyte nuclear factor-1α (HNF-1α).
Luis M. Real Hernandez
Junfeng Fan
Michelle H. Johnson
Elvira Gonzalez de Mejia
10.1371/journal.pone.0138768.g003
https://plos.figshare.com/articles/figure/_Interactions_between_delphinidin_3_O_arabinoside_and_a_homodimer_of_the_dimerization_domain_of_hepatocyte_nuclear_factor_1_HNF_1_/1558896
<p>The conformation of delphinidin-3-<i>O</i>-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-<i>O</i>-arabinoside (B). A hydrogen bond between atoms in the main-chain of SER6 and delphinidin-3-<i>O</i>-arabinoside is represented by a one headed, dashed green arrow. A 3-dimensional representation of delphinidin-3-<i>O</i>-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.</p>
2015-09-28 03:17:21
colon cells
expression
hnf
docking program AutoDock Vina
blackberry anthocyanin extracts
berry phenolic compounds
type II diabetes
Normal Colon Cells
dimerization domain