Revealing Molecular Coupling between Anion Selectivity and Structural Transitions in Voltage-Dependent Anion Channel (VDAC)

Involvement of voltage-dependent anion channel (VDAC) in dengue infection

During infection, dengue virus (DENV) proteins interact with host cellular constituents promoting the remodeling of the cell to facilitate virus production. While a number of interacting proteins have been identified for DENV non-structural proteins, far fewer interacting partners have been identified for the DENV structural proteins. One protein that has been identified as a DENV E protein int...

A 3D model of the voltage-dependent anion channel (VDAC).

Eukaryotic porins are a group of membrane proteins whose best known role is to form an aqueous pore channel in the mitochondrial outer membrane. As opposed to the bacterial porins (a large family of protein whose 3D structure has been determined by X-ray diffraction), the structure of eukaryotic porins (also termed VDACs, voltage-dependent anion-selective channels) is still a matter of debate. ...

Structural basis of the mitochondrial voltage-dependent anion channel VDAC I

The voltage-dependent anion channel (VDAC): function in intracellular signalling, cell life and cell death.

Research over the last decade has extended the prevailing view of mitochondria to include functions well beyond the critical bioenergetics role in supplying ATP. It is now recognized that mitochondria play a crucial role in cell signaling events, inter-organelle communication, aging, many diseases, cell proliferation and cell death. Apoptotic signal transmission to the mitochondria results in t...

Atlas of Genetics and Cytogenetics in Oncology and Haematology VDAC 1 ( voltage - dependent anion channel 1 )

Voltage-dependent anion-selective channel protein 1 (VDAC1, accession number: NP_003365.1) encodes for a protein product length of 283. VDAC1 regulates the flux of mostly anionic metabolites through the outer mitochondrial membrane, which is highly permeable to small molecules. VDAC is the most abundant protein in the outer membrane. Changes in membrane potentials can switch VDAC between open o...