1lmr

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(New page: 200px<br /><applet load="1lmr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lmr" /> '''Solution of ADO1, a Toxin from the Assassin ...)
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[[Image:1lmr.gif|left|200px]]<br /><applet load="1lmr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lmr" />
 
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'''Solution of ADO1, a Toxin from the Assassin Bugs Agriosphodrus dohrni that Blocks the Voltage Sensitive Calcium Channel L-type'''<br />
 
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==Overview==
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==Solution of ADO1, a Toxin from the Assassin Bugs Agriosphodrus dohrni that Blocks the Voltage Sensitive Calcium Channel L-type==
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ADO1 is a toxin purified from the saliva of the assassin bug, Agriosphodrus dohrni. Because of its similarity in sequence to Ptu1 from, another assassin bug, we did not assess its pharmacologic target. Here, we, demonstrate by electrophysiologic means that ADO1 targets the P/Q-type, voltage-sensitive calcium channel. We also determine the solution, structure of ADO1 using two-dimensional NMR techniques, followed by, distance geometry and molecular dynamics. The structure of ADO1 belongs to, the inhibitory cystine knot (ICK) structural family (i.e., a compact, disulfide-bonded core from which four loops emerge). ADO1 contains a, two-stranded, antiparallel beta-sheet structure. We compare the structure, of ADO1 with other voltage-sensitive calcium-channel blockers, analyze the, topologic juxtaposition of key functional residues, and conclude that the, recognition of voltage-sensitive calcium channels by toxins belonging to, the ICK structural family requires residues located on two distinct areas, of the molecular surface of the toxins.
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<StructureSection load='1lmr' size='340' side='right'caption='[[1lmr]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lmr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agriosphodrus_dohrni Agriosphodrus dohrni]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LMR 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, 21 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmr OCA], [https://pdbe.org/1lmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lmr RCSB], [https://www.ebi.ac.uk/pdbsum/1lmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lmr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PLK1_AGRDO PLK1_AGRDO] Binds reversibly and blocks P/Q-type voltage-gated calcium channels (Cav).<ref>PMID:14696181</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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ADO1 is a toxin purified from the saliva of the assassin bug, Agriosphodrus dohrni. Because of its similarity in sequence to Ptu1 from another assassin bug, we did not assess its pharmacologic target. Here, we demonstrate by electrophysiologic means that ADO1 targets the P/Q-type voltage-sensitive calcium channel. We also determine the solution structure of ADO1 using two-dimensional NMR techniques, followed by distance geometry and molecular dynamics. The structure of ADO1 belongs to the inhibitory cystine knot (ICK) structural family (i.e., a compact disulfide-bonded core from which four loops emerge). ADO1 contains a two-stranded, antiparallel beta-sheet structure. We compare the structure of ADO1 with other voltage-sensitive calcium-channel blockers, analyze the topologic juxtaposition of key functional residues, and conclude that the recognition of voltage-sensitive calcium channels by toxins belonging to the ICK structural family requires residues located on two distinct areas of the molecular surface of the toxins.
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==About this Structure==
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Solution structure of ADO1, a toxin extracted from the saliva of the assassin bug, Agriosphodrus dohrni.,Bernard C, Corzo G, Adachi-Akahane S, Foures G, Kanemaru K, Furukawa Y, Nakajima T, Darbon H Proteins. 2004 Feb 1;54(2):195-205. PMID:14696181<ref>PMID:14696181</ref>
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1LMR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agriosphodrus_dohrni Agriosphodrus dohrni]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LMR OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Solution structure of ADO1, a toxin extracted from the saliva of the assassin bug, Agriosphodrus dohrni., Bernard C, Corzo G, Adachi-Akahane S, Foures G, Kanemaru K, Furukawa Y, Nakajima T, Darbon H, Proteins. 2004 Feb 1;54(2):195-205. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14696181 14696181]
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</div>
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<div class="pdbe-citations 1lmr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Agriosphodrus dohrni]]
[[Category: Agriosphodrus dohrni]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Adachi-Akahane, S.]]
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[[Category: Adachi-Akahane S]]
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[[Category: Bernard, C.]]
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[[Category: Bernard C]]
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[[Category: Corzo, G.]]
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[[Category: Corzo G]]
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[[Category: Darbon, H.]]
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[[Category: Darbon H]]
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[[Category: Foures, G.]]
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[[Category: Foures G]]
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[[Category: Furukawa, Y.]]
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[[Category: Furukawa Y]]
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[[Category: Kanemaru, K.]]
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[[Category: Kanemaru K]]
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[[Category: Nakajima, T.]]
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[[Category: Nakajima T]]
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[[Category: ick]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:41:02 2007''
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Current revision

Solution of ADO1, a Toxin from the Assassin Bugs Agriosphodrus dohrni that Blocks the Voltage Sensitive Calcium Channel L-type

PDB ID 1lmr

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