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The VDAC Family [Function: Specific diffusion channels] Seed alignment | Full alignment | Pfam Wiki page | ||||
The voltage-dependent anion channel protein (VDAC) is the main protein of the mitochondrial outer membrane of all eukaryotes. VDAC regulates the movement of metabolites from the cytoplasm to the mitochondrion and vice-versa. Through this function, VDAC organizes various cellular processes like metabolism, apoptosis, calcium homeostasis and thus has an effect on a lot of diseases such as cancer, cardiovascular and neurodegenerative diseases. VDAC forms a ß barrel architecture constituted of 19 ß strands. | ||||
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| Literature references | ||||
Evaluation of the ß-barrel outer membrane protein VP1243 as a candidate antigen for a cross-protective vaccine against Vibrio infections Microb Pathog. 2020 Oct;147:104419. doi: 10.1016/j.micpath.2020.104419. Epub 2020 Aug 5. PMID: 32768517 | ||||
Landscape of Eukaryotic Transmembrane Beta Barrel Proteins J Proteome Res. 2020 Mar 6;19(3):1209-1221. doi: 10.1021/acs.jproteome.9b00740. Epub 2020 Feb 11. PMID: 32008325 | ||||
Helix-strand interaction regulates stability and aggregation of the human mitochondrial membrane protein channel VDAC3 J Gen Physiol. 2019 Apr 1;151(4):489-504. doi: 10.1085/jgp.201812272. Epub 2019 Jan 23. PMID: 30674561 | ||||
Identification of a novel vaccine candidate by immunogenic screening of Vibrio parahaemolyticus outer membrane proteins Vaccine. 2014 Oct 21;32(46):6115-21. doi: 10.1016/j.vaccine.2014.08.077. Epub 2014 Sep 16. PMID: 25236587 | ||||
Influence of protein-micelle ratios and cysteine residues on the kinetic stability and unfolding rates of human mitochondrial VDAC-2 PLoS One. 2014 Jan 29;9(1):e87701. doi: 10.1371/journal.pone.0087701. eCollection 2014. PMID: 24494036 | ||||
The structural biology of ß-barrel membrane proteins: a summary of recent reports Curr Opin Struct Biol. 2011 Aug;21(4):523-31. doi: 10.1016/j.sbi.2011.05.005. Epub 2011 Jun 28. PMID: 21719274 | ||||
| Proteins in this family with 3D-structure | ||||
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