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Title:
Toward the molecular structure of the mitochondrial channel, VDAC | Journal of Bioenergetics and Biomembranes
Description:
A summary is presented of the most recent information about the structure and mechanism of closure of the mitochondrial channel, VDAC. Considerable information has come from studies involving electron microscopy of two-dimensional crystals and from electrophysiological studies of wild-type channels and site-directed mutants. Available evidence points to a Ξ²-barrel as the basic structural model for VDAC. Two models for voltage- or effector- induced closure have been proposed, the first involving removal of strands from the wall of the pore, the second invoking movement of protein domains into the lumen. Experimental strategies to resolve the actual mechanism are presented.
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headline:Toward the molecular structure of the mitochondrial channel, VDAC
description:A summary is presented of the most recent information about the structure and mechanism of closure of the mitochondrial channel, VDAC. Considerable information has come from studies involving electron microscopy of two-dimensional crystals and from electrophysiological studies of wild-type channels and site-directed mutants. Available evidence points to a Ξ²-barrel as the basic structural model for VDAC. Two models for voltage- or effector- induced closure have been proposed, the first involving removal of strands from the wall of the pore, the second invoking movement of protein domains into the lumen. Experimental strategies to resolve the actual mechanism are presented.
datePublished:
dateModified:
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VDAC
membrane channel
voltage gating
electron microscopy
membrane crystals
site-directed mutagenesis
Bioorganic Chemistry
Biochemistry
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Animal Anatomy / Morphology / Histology
Animal Biochemistry
Organic Chemistry
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headline:Toward the molecular structure of the mitochondrial channel, VDAC
description:A summary is presented of the most recent information about the structure and mechanism of closure of the mitochondrial channel, VDAC. Considerable information has come from studies involving electron microscopy of two-dimensional crystals and from electrophysiological studies of wild-type channels and site-directed mutants. Available evidence points to a Ξ²-barrel as the basic structural model for VDAC. Two models for voltage- or effector- induced closure have been proposed, the first involving removal of strands from the wall of the pore, the second invoking movement of protein domains into the lumen. Experimental strategies to resolve the actual mechanism are presented.
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Mitochondrial outer membrane
VDAC
membrane channel
voltage gating
electron microscopy
membrane crystals
site-directed mutagenesis
Bioorganic Chemistry
Biochemistry
general
Animal Anatomy / Morphology / Histology
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Organic Chemistry
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