Positive allosteric modulators of lecithin: Cholesterol acyltransferase adjust the orientation of the membrane-binding domain and alter its spatial free energy profile
Fig 3
(A) The average number of hydrogen bonds formed between the MBD amino acids and drug compounds during the whole simulation trajectory. (B) The average number of hydrophobic interactions between drugs and amino acids showing the most variation for compound 8 relative to other compounds. (C) Visualization of the primary hydrogen bonding pairs between compounds and LCAT. Snapshots from Drug-1B (Top) and Drug-2A (Bottom) simulations showing the conformations of compounds 1b and 2a in the cleft of MBD. The hydrogen bonds between drugs and amino acids are marked with black dashed lines. Compounds 1b and 2a are rendered as sticks and are colored according to the element types. Compound 1b is hued purple and 2a orange. The MBD cleft is rendered as a cartoon representation and colored green. Amino acids forming hydrogen bonds with compounds are rendered as sticks and colored according to the element types. Carbon atoms are cyan, oxygen red, nitrogen blue, fluorine pink, and sulfur yellow.