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Human VDAC

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.


Structure of the human voltage-dependent anion channel.

Bayrhuber M1, Meins T, Habeck M, Becker S, Giller K, Villinger S, Vonrhein C, Griesinger C, Zweckstetter M, Zeth K.

Proc Natl Acad Sci U S A. 2008 Oct 7;105(40):15370-5. doi: 10.1073/pnas.0808115105. Epub 2008 Oct 1.  (PubMed)

2JK4 (PDB)

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