1amt
A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION
OverviewOverview
The crystal structure of alamethicin in nonaqueous solvent has been determined, and refined at 1.5-A resolution. The molecular conformation of the three crystallographically independent molecules is largely alpha-helical with a bend in the helix axis at an internal proline residue. The helix structure is highly amphipathic as most of the solvent-accessible polar atoms lie on a narrow strip of surface parallel to the helix axis. Molecular models for the voltage-gated ion channel, with n-fold symmetry and based on the molecular conformations observed in the crystal, are characterized by strong surface complementarity, a hydrophilic interior and a hydrophobic exterior. The channel structures are stabilized by a hydrated annulus of hydrogen-bonded glutamine residues which produce the greatest restriction in the channel diameter.
About this StructureAbout this Structure
Full crystallographic information is available from OCA.
ReferenceReference
A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution., Fox RO Jr, Richards FM, Nature. 1982 Nov 25;300(5890):325-30. PMID:6292726 Page seeded by OCA on Fri May 2 10:27:48 2008