2JK4

Structure of the human voltage-dependent anion channel

2JK4 の概要

• エントリーDOI: 10.2210/pdb2jk4/pdb
• 分子名称: VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL PROTEIN 1 (1 entity in total)
• 機能のキーワード: vdac, porin, membrane, apoptosis, transport, mitochondrion outer membrane, mitochondrial outer membrane, membrane protein, host-virus interaction, ion transport, transmembrane, phosphoprotein, acetylation, mitochondrion, cell membrane
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32181.99

構造登録者

Bayrhuber, M.,Meins, T.,Habeck, M.,Becker, S.,Giller, K.,Villinger, S.,Vonrhein, C.,Griesinger, C.,Zweckstetter, M.,Zeth, K. (登録日: 2008-08-15, 公開日: 2008-10-14, 最終更新日: 2024-05-08)

主引用文献

Bayrhuber, M.,Meins, T.,Habeck, M.,Becker, S.,Giller, K.,Villinger, S.,Vonrhein, C.,Griesinger, C.,Zweckstetter, M.,Zeth, K.
Structure of the Human Voltage-Dependent Anion Channel.
Proc.Natl.Acad.Sci.USA, 105:15370-, 2008

PubMed Abstract: 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 beta-barrel architecture composed of 19 beta-strands with an alpha-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.

PubMed: 18832158
DOI: 10.1073/PNAS.0808115105

実験手法

X-RAY DIFFRACTION (4.1 Å)