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- W2040787543 abstract "The Voltage Dependent Anion Channel (VDAC) constitutes the major pathway for the entry and exit of metabolites across the outer membrane of the mitochondria and can serve as a scaffold for molecules that modulate the organelle. After decades of trials, three groups independently reported the 3D structure of this eukaryotic membrane protein consisting of a 19-stranded β-barrel. Our group resolved the mVDAC1 structure at 2.3Å resolution revealing a high-resolution image of its architecture including the position of the voltage sensing N-terminal α-helix segment- oriented against the interior wall causing a partial narrowing at the center of the pore. Recently, however, the overall relevance of these structures and whether they represent a native conformation has been called into question. This presentation will highlight our assertion that this fold is indeed the native structure and stress: a) the bicelle crystallization method, b) electrostatic experiments corroborating an ‘open’ conformation, and c) new ongoing experiments to validate gating and conformation observed in the crystal structure." @default.
- W2040787543 created "2016-06-24" @default.
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- W2040787543 date "2010-01-01" @default.
- W2040787543 modified "2023-09-26" @default.
- W2040787543 title "The Crystal Structure of the Murine Voltage Dependent Anion Channel 1 (mVDAC1) (Likely) Represents a Native Conformation" @default.
- W2040787543 doi "https://doi.org/10.1016/j.bpj.2009.12.1108" @default.
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