期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1818, 期 6, 页码 1562-1569出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2011.11.012
关键词
VDAC; Mitochondrion; NMR spectroscopy; Micelle; Nanodisc; Membrane protein
资金
- National Science Council in Taiwan [NSC98-2917-I-564-157]
- NIH [GM075879, GM047467, S10 RR026417, EB002026]
- Swiss National Science Foundation
- ERC [MOMP 281764]
- Taplin Fund for Discovery
Three isoforms of the human voltage-dependent anion channel (VDAC), located in the outer mitochondrial membrane, are crucial regulators of mitochondrial function. Numerous studies have been carried out to elucidate biochemical properties, as well as the three-dimensional structure of VDAC-1. However, functional and structural studies of VDAC-2 and VDAC-3 at atomic resolution are still scarce. VDAC-2 is highly similar to VDAC-1 in amino acid sequence, but has substantially different biochemical functions and expression profiles. Here, we report the reconstitution of functional VDAC-2 in lauryldimethylamine-oxide (LDAO) detergent micelles and 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) lipid bilayer nanodiscs. We find that VDAC-2 is properly folded in both membrane-mimicking systems and that structural and functional characterization by solution NMR spectroscopy is feasible. This article is part of a Special Issue entitled: VDAC structure, function, and regulation of mitochondrial metabolism. (C) 2011 Elsevier BM. All rights reserved.
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