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N-Terminal
Helix Is Located Inside the Pore.
The N-terminal
helix comprising residues Tyr-7 to Val-17 is folded
horizontally inside the barrel wall approximately at the
midpoint of the hydrophobic portion of the membrane.
Dimerization
of VDAC via a Small Hydrophobic Interface.
The interface provided by residues
in β-strands β1 (Ile-30,Leu-32), β2 (Glu-53,Thr-54), β18
(Leu-260,Leu-262), and β19 (Leu-280).
Conformational
Instability of the N-Terminal Part of hVDAC1.
The structural instability of the N-terminal part is
particularly influenced by Glu-76.
This residue is conserved in different isoforms of human VDAC and
in VDAC from mammals and fungi. In the 3D structure, Glu-76
points to the membrane and interrupts the amphipathic pattern in β
strand 4.
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