Backbone and ILV side chain methyl group assignments of the integral human membrane protein VDAC-1.
The voltage dependent anion channel (VDAC) forms a channel for metabolites and nutrients in the outer membrane of mitochondria, and it is also involved in apoptotic pathways. Here, we report sequence-specific NMR assignments for the isoform 1 of human VDAC reconstituted in lauryldimethylamine oxide (LDAO) detergent micelles. The assignments were deposited in the BMRB data base with accession number 16381.
Hiller
Sebastian
S
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Malia
Thomas J
TJ
Garces
Robert G
RG
Orekhov
Vladislav Y
VY
Wagner
Gerhard
G
D030562:Databases, Protein; D004123:Dimethylamines; D006801:Humans; D008823:Micelles; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D020033:Protein Isoforms / Q000737:chemistry; D017433:Protein Structure, Secondary; D050995:Voltage-Dependent Anion Channel 1 / Q000737:chemistry*
D004123:Dimethylamines; D008823:Micelles; D020033:Protein Isoforms; C494762:VDAC1 protein, human; C014518:dodecyldimethylamine oxide; D050995:Voltage-Dependent Anion Channel 1