Figure 5
From: Binding site of ABC transporter homology models confirmed by ABCB1 crystal structure
Comparison of proposed drug binding site in ABCB1 model (A) and the drug binding site in the X-ray crystal structure of P-glycoprotein (ABCB1) [20] (B) viewed from the intracellular side with amino acids suggested from site directed mutagenesis studies to take part in ligand binding displayed as sticks coloured according to atom type (C = grey; H = dark grey; O = red; N = blue); Ile306 (TMH5) [27, 35], Ile340 (TMH6) [33], Phe343 (TMH6) [21, 27], Phe728 (TMH7) [27], and Val982 (TMH12) [33, 35]. Amino acids in panel B are numbered according to human ABCB1. Mus musculus numbering: Ile302, Ile336, Phe339 Phe724 and Val978. Differences in helix tilting in the panels refer to the different conformations of ABCB1, outward facing conformation in the left panel and closed conformation in the right panel.