1amt

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(New page: 200px<br /><applet load="1amt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1amt, resolution 1.5&Aring;" /> '''A VOLTAGE-GATED ION C...)
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caption="1amt, resolution 1.5&Aring;" />
caption="1amt, resolution 1.5&Aring;" />
'''A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION'''<br />
'''A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1AMT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ACE, CCN and MOH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AMT OCA].
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1AMT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene>, <scene name='pdbligand=CCN:'>CCN</scene> and <scene name='pdbligand=MOH:'>MOH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMT OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=6292726 6292726]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=6292726 6292726]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Fox, R.O.]]
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[[Category: Fox, R O.]]
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[[Category: Richards, F.M.]]
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[[Category: Richards, F M.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: CCN]]
[[Category: CCN]]
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[[Category: peptide antibiotic]]
[[Category: peptide antibiotic]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:05:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:12 2008''

Revision as of 09:46, 21 February 2008

Image:1amt.jpg

1amt, resolution 1.5Å

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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 , and 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 Thu Feb 21 11:46:12 2008

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