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1amt
From Proteopedia
(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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| - | [[Image:1amt.jpg|left|200px]]<br /><applet load="1amt" size=" | + | [[Image:1amt.jpg|left|200px]]<br /><applet load="1amt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1amt, resolution 1.5Å" /> | caption="1amt, resolution 1.5Å" /> | ||
'''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== | ||
| - | The crystal structure of alamethicin in nonaqueous solvent has been | + | 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== | ||
| - | 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:// | + | 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]] | ||
| - | [[Category: Fox, R | + | [[Category: Fox, R O.]] |
| - | [[Category: Richards, F | + | [[Category: Richards, F M.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: CCN]] | [[Category: CCN]] | ||
| Line 19: | Line 19: | ||
[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
| - | ''Page seeded by [http:// | + | ''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
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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
Categories: Protein complex | Fox, R O. | Richards, F M. | ACE | CCN | MOH | Peptide antibiotic
