2a9h: Difference between revisions
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'''NMR structural studies of a potassium channel / charybdotoxin complex''' | {{Structure | ||
|PDB= 2a9h |SIZE=350|CAPTION= <scene name='initialview01'>2a9h</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= kcsA, skc1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans]) | |||
}} | |||
'''NMR structural studies of a potassium channel / charybdotoxin complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2A9H is a [ | 2A9H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A9H OCA]. | ||
==Reference== | ==Reference== | ||
Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex., Yu L, Sun C, Song D, Shen J, Xu N, Gunasekera A, Hajduk PJ, Olejniczak ET, Biochemistry. 2005 Dec 6;44(48):15834-41. PMID:[http:// | Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex., Yu L, Sun C, Song D, Shen J, Xu N, Gunasekera A, Hajduk PJ, Olejniczak ET, Biochemistry. 2005 Dec 6;44(48):15834-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16313186 16313186] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces lividans]] | [[Category: Streptomyces lividans]] | ||
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[[Category: structure]] | [[Category: structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:47:00 2008'' | ||
Revision as of 16:47, 20 March 2008
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| Gene: | kcsA, skc1 (Streptomyces lividans) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR structural studies of a potassium channel / charybdotoxin complex
OverviewOverview
Ion channels play critical roles in signaling processes and are attractive targets for treating various diseases. Here we describe an NMR-based strategy for structural analyses of potassium channel-ligand complexes using KcsA (residues 1-132, with six mutations to impart toxin binding and to mimic the eukaryotic hERG channel). Using this approach, we determined the solution structure of KcsA in complex with the high-affinity peptide antagonist charybdotoxin. The structural data reveal how charybdotoxin binds to the closed form of KcsA and makes specific contacts with the extracellular surface of the ion channel, resulting in pore blockage. This represents the first direct structural information about an ion channel complexed to a peptide antagonist and provides an experimental framework for understanding and interpreting earlier mutational analyses. The strategy presented here overcomes many of the limitations of conventional NMR approaches to helical membrane protein structure determination and can be applied in the study of the binding of druglike molecules to this important class of proteins.
About this StructureAbout this Structure
2A9H is a Single protein structure of sequence from Streptomyces lividans. Full crystallographic information is available from OCA.
ReferenceReference
Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex., Yu L, Sun C, Song D, Shen J, Xu N, Gunasekera A, Hajduk PJ, Olejniczak ET, Biochemistry. 2005 Dec 6;44(48):15834-41. PMID:16313186
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