Molecular dynamics simulations of the Cx26 hemichannel: evaluation of structural models with Brownian dynamics.

ABSTRACT: The recently published crystal structure of the Cx26 gap junction channel provides a unique opportunity for elucidation of the structure of the conductive connexin pore and the molecular determinants of its ion permeation properties (conductance, current-voltage [I-V] relations, and charge selectivity). However, the crystal structure was incomplete, most notably lacking the coordinates of the N-terminal methionine residue, which resides within the pore, and also lacking two cytosolic domains. To allow computational studies for comparison with the known channel properties, we completed the structure. Grand canonical Monte Carlo Brownian dynamics (GCMC/BD) simulations of the completed and the published Cx26 hemichannel crystal structure indicate that the pore is too narrow to permit signific

SUBMITTER: Kwon T 

PROVIDER: S-EPMC3206306 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature