VDAC1 (voltage-dependent anion channel 1) selectivity in physiological salt concentrations

Range ~5 Cl−/K+
Organism Mitochondria
Reference Choudhary OP, Paz A, Adelman JL, Colletier JP, Abramson J, Grabe M. Structure-guided simulations illuminate the mechanism of ATP transport through VDAC1. Nat Struct Mol Biol. 2014 Jul21(7):626-32. doi: 10.1038/nsmb.2841 p.628 left column 2nd paragraphPubMed ID24908397
Primary Source [29] Colombini M. VDAC structure, selectivity, and dynamics. Biochim Biophys Acta. 2012 Jun1818(6):1457-65. doi: 10.1016/j.bbamem.2011.12.026PubMed ID22240010
Method Abstract: "To understand ATP permeation through VDAC, [investigators] solved the crystal structure of mouse VDAC1 (mVDAC1) in the presence of ATP, revealing a low-affinity binding site. Guided by these coordinates, [they] initiated hundreds of molecular dynamics simulations to construct a Markov state model of ATP permeation."
Comments P.628 left column 2nd paragraph: "[Investigators’] calculations recapitulate the experimental finding that VDAC1 selectivity is ~5 (Cl−/K+) in physiological salt concentrations [primary source] and 1.7–1.9 under a 1.0–0.1 M KCl gradient [ref 15]."
Entered by Uri M
ID 116876