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Human VDAC

Cholesterol binding sites on mitochondrial VDAC.
Site 1: Lys 99, Thr 119, Gly 120, Asp 131
Site 2: Phe 172, Ala 173
Site 3: Gly 175
Site 4: Lys 239
Site 5: Ser 263
 N-terminal domain.
The N-terminal α-helical segment is proposed to be involved in channel gating, where it could be acting as the voltage sensor and possibly regulating the conductance of ions and metabolites through the VDAC1 pore.
VDAC1-N-terminus is required for apoptosis induction, its interaction with HK-I and Bcl2 has a protective effect against apoptosis.   Mutations.
K237 and K239 mutations impaires the ability of the voltage-dependent anion channel (VDAC1) to insert into the outer membrane of the mitochondria .



1. Computational Investigation of Cholesterol Binding Sites on Mitochondrial VDAC.

Brian P. Weiser, Reza Salari, Roderic G. Eckenhoff, and Grace Brannigan

J Phys Chem B. 2014 Aug 21;118(33):9852-60. doi: 10.1021/jp504516a. Epub 2014 Aug 11. (PubMed)



2. The VDAC1 N-terminus is essential both for apoptosis and the protective effect of anti-apoptotic proteins.

Abu-Hamad S, Arbel N, Calo D, Arzoine L, Israelson A, Keinan N, Ben-Romano R, Friedman O, Shoshan-Barmatz V

J Cell Sci. 2009 Jun 1;122(Pt 11):1906-16. doi: 10.1242/jcs.040188. (PubMed)



3. Mutation of K234 and K236 in the voltage-dependent anion channel 1 impairs its insertion into the mitochondrial outer membrane.

Angeles R, Devine J, Barton K, Smith M, McCauley R.

J Bioenerg Biomembr. 1999 Apr;31(2):137-42. (PubMed)

2JK4 (PDB)

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