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| {{STRUCTURE_1m24| PDB=1m24 | SCENE= }} | | {{STRUCTURE_1m24| PDB=1m24 | SCENE= }} |
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| '''Trichotoxin_A50E, An Ion Channel-Forming Polypeptide'''
| | ===Trichotoxin_A50E, An Ion Channel-Forming Polypeptide=== |
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| ==Overview==
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| Trichotoxin_A50E is an 18-residue peptaibol antibiotic which forms multimeric transmembrane channels through self-association. The crystal structure of trichotoxin has been determined at a resolution of 0.9 A. The trichotoxin sequence contains nine helix-promoting Aib residues, which contribute to the formation of an entirely helical structure that has a central bend of 8-10 degrees located between residues 10-13. Trichotoxin is the first solved structure of the peptaibol family that is all alpha-helix as opposed to containing part or all 3(10)-helix. Gln residues in positions 6 and 17 produce a polar face, and are proposed to form the channel lumen. An octameric model channel has been constructed from the crystal structure. It has a central pore of approximately 4-5 A radius, a size sufficient to enable transport of ions, with a constricted region at one end, formed by a ring of Gln6 residues. Electrostatic calculations are consistent with it being a cationic channel.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12390019}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12390019 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12390019}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ion channel]] | | [[Category: Ion channel]] |
| [[Category: Peptaibol]] | | [[Category: Peptaibol]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:32:40 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:03:37 2008'' |