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1agt

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[[Image:1agt.gif|left|200px]]
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{{Structure
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|GENE= AGTX2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6884 Leiurus quinquestriatus hebraeus])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1agt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1agt OCA], [http://www.ebi.ac.uk/pdbsum/1agt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1agt RCSB]</span>
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'''SOLUTION STRUCTURE OF THE POTASSIUM CHANNEL INHIBITOR AGITOXIN 2: CALIPER FOR PROBING CHANNEL GEOMETRY'''
'''SOLUTION STRUCTURE OF THE POTASSIUM CHANNEL INHIBITOR AGITOXIN 2: CALIPER FOR PROBING CHANNEL GEOMETRY'''
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[[Category: Mackinnon, R.]]
[[Category: Mackinnon, R.]]
[[Category: Wagner, G.]]
[[Category: Wagner, G.]]
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[[Category: potassium channel blocker]]
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[[Category: Potassium channel blocker]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:15:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:39:56 2008''
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Revision as of 07:15, 2 May 2008

Template:STRUCTURE 1agt

SOLUTION STRUCTURE OF THE POTASSIUM CHANNEL INHIBITOR AGITOXIN 2: CALIPER FOR PROBING CHANNEL GEOMETRY


Overview

The structure of the potassium channel blocker agitoxin 2 was solved by solution NMR methods. The structure consists of a triple-stranded antiparallel beta-sheet and a single helix covering one face of the beta-sheet. The cysteine side chains connecting the beta-sheet and the helix form the core of the molecule. One edge of the beta-sheet and the adjacent face of the helix form the interface with the Shaker K+ channel. The fold of agitoxin is homologous to the previously determined folds of scorpion venom toxins. However, agitoxin 2 differs significantly from the other channel blockers in the specificity of its interactions. This study was thus focused on a precise characterization of the surface residues at the face of the protein interacting with the Shaker K+ channel. The rigid toxin molecule can be used to estimate dimensions of the potassium channel. Surface-exposed residues, Arg24, Lys27, and Arg31 of the beta-sheet, have been identified from mutagenesis studies as functionally important for blocking the Shaker K+ channel. The sequential and spatial locations of Arg24 and Arg31 are not conserved among the homologous toxins. Knowledge on the details of the channel-binding sites of agitoxin 2 formed a basis for site-directed mutagenesis studies of the toxin and the K+ channel sequences. Observed interactions between mutated toxin and channel are being used to elucidate the channel structure and mechanisms of channel-toxin interactions.

About this Structure

1AGT is a Single protein structure of sequence from Leiurus quinquestriatus hebraeus. Full crystallographic information is available from OCA.

Reference

Solution structure of the potassium channel inhibitor agitoxin 2: caliper for probing channel geometry., Krezel AM, Kasibhatla C, Hidalgo P, MacKinnon R, Wagner G, Protein Sci. 1995 Aug;4(8):1478-89. PMID:8520473 Page seeded by OCA on Fri May 2 10:15:01 2008

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