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1amt
From Proteopedia
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(New page: 200px<br /><applet load="1amt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1amt, resolution 1.5Å" /> '''A VOLTAGE-GATED ION C...)
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Revision as of 20:57, 24 November 2007
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A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION
Overview
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 Structure
1AMT is a Protein complex structure of sequences from [1] with ACE, CCN and MOH as ligands. Full crystallographic information is available from OCA.
Reference
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 Sat Nov 24 23:05:20 2007
Categories: Protein complex | Fox, R.O. | Richards, F.M. | ACE | CCN | MOH | Peptide antibiotic
