Porin or voltage-dependent anion-selective channel (VDAC) is the main protein responsible for the high permeability of the outer mitochondrial membrane. The mitochondrial porin is mainly composed of sided beta-strands, in analogy with bacterial porin, whose structure has been resolved at 1.8 angstrom resolution. In mitochondrial porins the N-terminal region forms an amphipathic alpha-helix, a structure conserved in organisms very distant from the evolutionary point of view. This part of the protein is exposed to the water phase, as demonstrated by ELISA assays. Various extramembranous loops have been identified by specific proteolytic cleavages. These overall, combined results were used to draw a model of the transmembrane arrangement of mammalian porin. This model is compared to other mitochondrial and bacterial porin models.
|Titolo:||TRANSMEMBRANE ARRANGEMENT OF MITOCHONDRIAL PORIN OR VOLTAGE-DEPENDENT ANION CHANNEL (VDAC)|
|Data di pubblicazione:||1992|
|Citazione:||TRANSMEMBRANE ARRANGEMENT OF MITOCHONDRIAL PORIN OR VOLTAGE-DEPENDENT ANION CHANNEL (VDAC) / DE PINTO V; PALMIERI F. - In: JOURNAL OF BIOENERGETICS AND BIOMEMBRANES. - ISSN 0145-479X. - 24:1(1992), pp. 21-26.|
|Appare nelle tipologie:||1.1 Articolo in rivista|