Functional analysis of human Na+/K+-ATPase familial or sporadic hemiplegic migraine mutations expressed in Xenopus oocytes

Figure 7 Structural details of the C-terminal region and α/β-interactions. A: Structural details (PDB structure entry 3B8E) of putative interactions between the α- and β-subunit. Interacting residues are shown as sticks. Tyr39 and Tyr43 in the β-transmembrane domain (green) can interact with αM7 (purple). The α-helix is unwound at residue Gly952 (αM7). Tyr851 can form hydrogen bonds to Asn780 in αM5 (marine), which is part of the K⁺ binding site I and II. Also shown is αM10 (light blue) with the C-terminus (orange) of the α-subunit; B: Structural details of the C-terminal region viewed from the intracellular side. Possibly interacting residues are shown in sticks. The C-terminal Tyr1019 and Tyr1020 (orange) can interact with Arg1002 in αM10 (light blue), Arg937 (αM8/M9-loop in purple) and Lys770 in αM5 (marine). Asp999 (αM10) can form hydrogen bonds to Arg1002. Lys1003 (αM10) is not involved in the C-terminal network.