Charged residues distribution modulates selectivity of the open state of human isoforms of the voltage dependent anion-selective channel.

ABSTRACT: Voltage Dependent Anion-selective Channels (VDACs) are pore-forming proteins located in the outer mitochondrial membrane. They are responsible for the access of ions and energetic metabolites into the inner membrane transport systems. Three VDAC isoforms exist in mammalian, but their specific role is unknown. In this work we have performed extensive (overall ∼5 µs) Molecular Dynamics (MD) simulations of the human VDAC isoforms to detect structural and conformational variations among them, possibly related to specific functional roles of these proteins. Secondary structure analysis of the N-terminal domain shows a high similarity among the three human isoforms of VDAC but with a different plasticity. In particular, the N-terminal domain of the hVDAC1 is characterized by a higher plasticity,

SUBMITTER: Amodeo GF 

PROVIDER: S-EPMC4146382 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature