1amt: Difference between revisions

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Revision as of 10:59, 20 March 2008

File:1amt.jpg

, resolution 1.5Å

Ligands:

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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

1AMT is a Protein complex structure of sequences from [1]. 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 Thu Mar 20 09:59:46 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1amt.jpg|left|200px]]<br /><applet load="1amt" size="350" color="white" frame="true" align="right" spinBox="true"
+[[Image:1amt.jpg|left|200px]]
-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 />
+ {{Structure
+|PDB= 1amt |SIZE=350|CAPTION= <scene name='initialview01'>1amt</scene>, resolution 1.5&Aring;
+|SITE=
+|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene> and <scene name='pdbligand=MOH:METHANOL'>MOH</scene>
+|ACTIVITY=
+|GENE=
+}}
+'''A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION'''
 ==Overview==
@@ Line 7: / Line 16: @@
 ==About this Structure==
-AMT 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].
+AMT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMT 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:[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://www.ncbi.nlm.nih.gov/pubmed/6292726 6292726]
 [[Category: Protein complex]]
 [[Category: Fox, R O.]]
@@ Line 19: / Line 28: @@
 [[Category: peptide antibiotic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:46 2008''