1av2: Difference between revisions

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[[Image:1av2.gif|left|200px]]
{{Seed}}
[[Image:1av2.png|left|200px]]


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{{STRUCTURE_1av2|  PDB=1av2  |  SCENE=  }}  
{{STRUCTURE_1av2|  PDB=1av2  |  SCENE=  }}  


'''GRAMICIDIN A/CSCL COMPLEX, ACTIVE AS A DIMER'''
===GRAMICIDIN A/CSCL COMPLEX, ACTIVE AS A DIMER===




==Overview==
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The linear pentadecapeptide antibiotic, gramicidin D, is a naturally occurring product of Bacillus brevis known to form ion channels in synthetic and natural membranes. The x-ray crystal structures of the right-handed double-stranded double-helical dimers (DSDH) reported here agree with 15N-NMR and CD data on the functional gramicidin D channel in lipid bilayers. These structures demonstrate single-file ion transfer through the channels. The results also indicate that previous crystal structure reports of a left-handed double-stranded double-helical dimer in complex with Cs+ and K+ salts may be in error and that our evidence points to the DSDH as the major conformer responsible for ion transport in membranes.
The line below this paragraph, {{ABSTRACT_PUBMED_9789021}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9789021 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9789021}}


==About this Structure==
==About this Structure==
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[[Category: Ion channel]]
[[Category: Ion channel]]
[[Category: Peptide antibiotic]]
[[Category: Peptide antibiotic]]
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