1amt
From Proteopedia
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| - | [[ | + | ==Crystal structure of alamethicin at 1.5 angstrom resolution== |
| + | <StructureSection load='1amt' size='340' side='right' caption='[[1amt]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1amt]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AMT FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=PHL:L-PHENYLALANINOL'>PHL</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m24|1m24]], [[1r9u|1r9u]], [[1dlz|1dlz]], [[1ih9|1ih9]], [[1gq0|1gq0]], [[1joh|1joh]], [[1ee7|1ee7]], [[1ob7|1ob7]], [[1ob6|1ob6]], [[1ob4|1ob4]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1amt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1amt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1amt RCSB], [http://www.ebi.ac.uk/pdbsum/1amt PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:6292726</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Fox, R O.]] | [[Category: Fox, R O.]] | ||
[[Category: Richards, F M.]] | [[Category: Richards, F M.]] | ||
Revision as of 08:12, 30 July 2014
Crystal structure of alamethicin at 1.5 angstrom resolution
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