1agt

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<StructureSection load='1agt' size='340' side='right'caption='[[1agt]]' scene=''>
<StructureSection load='1agt' size='340' side='right'caption='[[1agt]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1agt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leiurus_quinquestriatus_hebraeus Leiurus quinquestriatus hebraeus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AGT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1agt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leiurus_hebraeus Leiurus hebraeus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AGT FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 17 models</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1agt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1agt OCA], [https://pdbe.org/1agt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1agt RCSB], [https://www.ebi.ac.uk/pdbsum/1agt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1agt ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1agt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1agt OCA], [https://pdbe.org/1agt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1agt RCSB], [https://www.ebi.ac.uk/pdbsum/1agt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1agt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/KAX32_LEIHE KAX32_LEIHE] Potent inhibitor of the Shaker potassium channels and its mammalian homologs (Kv1.1/KCNA1, Kv1.3/KCNA3, Kv1.6/KCNA6) (Ki<1 nM for all channels) (PubMed:8204618, PubMed:20007782). Also blocks Kv1.2/KCNA2 (IC(50)=26.8 nM) (PubMed:8204618, PubMed:20007782). It also shows a weak interaction with nicotinic acetylcholine receptors (nAChR), suggesting it may weakly inhibit it (PubMed:31276191).<ref>PMID:20007782</ref> <ref>PMID:8204618</ref>
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[https://www.uniprot.org/uniprot/KAX32_LEIHE KAX32_LEIHE] Potent inhibitor of the Shaker potassium channels and its mammalian homologs (Kv1.1/KCNA1, Kv1.3/KCNA3, Kv1.6/KCNA6) (Ki<1 nM for all channels) (PubMed:20007782, PubMed:8204618). Also blocks Kv1.2/KCNA2 (IC(50)=26.8 nM) (PubMed:20007782, PubMed:8204618). It also shows a weak interaction with nicotinic acetylcholine receptors (nAChR), suggesting it may weakly inhibit it (PubMed:31276191).<ref>PMID:20007782</ref> <ref>PMID:8204618</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ag/1agt_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ag/1agt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1agt ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1agt ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:8520473</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1agt" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Leiurus quinquestriatus hebraeus]]
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[[Category: Leiurus hebraeus]]
[[Category: Hidalgo P]]
[[Category: Hidalgo P]]
[[Category: Kasibhatla C]]
[[Category: Kasibhatla C]]

Current revision

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

PDB ID 1agt

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