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          Institute: MPI für biologische Kybernetik     Collection: Biologische Kybernetik     Display Documents



ID: 419876.0, MPI für biologische Kybernetik / Biologische Kybernetik
Structure of the human voltage-dependent anion channel
Authors:Bayrhuber, M.; Meins, T.; Habeck, M.; Becker, S.; Giller, K.; Villinger, S.; Vonrhein, C.; Griesinger, C.; Zweckstetter, M.; Zeth, K.
Date of Publication (YYYY-MM-DD):2008-10
Title of Journal:Proceedings of the National Academy of Sciences of the United States of America
Volume:105
Issue / Number:40
Start Page:15370
End Page:15375
Audience:Not Specified
Intended Educational Use:No
Abstract / Description:The voltage-dependent anion channel (VDAC), also known as mitochondrial porin, is the most abundant protein in the mitochondrial outer membrane (MOM). VDAC is the channel known to guide the metabolic flux across the MOM and plays a key role in mitochondrially induced apoptosis. Here, we present the 3D structure of human VDAC1, which was solved conjointly by NMR spectroscopy and x-ray crystallography. Human VDAC1 (hVDAC1) adopts a β-barrel architecture composed of 19 β-strands with an α-helix located horizontally midway within the pore. Bioinformatic analysis indicates that this channel architecture is common to all VDAC proteins and is adopted by the general import pore TOM40 of mammals, which is also located in the MOM.
External Publication Status:published
Document Type:Article
Communicated by:Holger Fischer
Affiliations:MPI f�r biologische Kybernetik/Empirical Inference (Dept. Sch�lkopf)
Identifiers:LOCALID:5523
URL:http://www.pnas.org/content/105/40/15370.full
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