2e2s: Difference between revisions

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==Solution structure of agelenin, an insecticidal peptide from the venom of Agelena opulenta==
==Solution structure of agelenin, an insecticidal peptide from the venom of Agelena opulenta==
<StructureSection load='2e2s' size='340' side='right' caption='[[2e2s]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2e2s' size='340' side='right'caption='[[2e2s]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2e2s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Allagelena_opulenta Allagelena opulenta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E2S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E2S FirstGlance]. <br>
<table><tr><td colspan='2'>[[2e2s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Allagelena_opulenta Allagelena opulenta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E2S FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e2s OCA], [http://pdbe.org/2e2s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e2s RCSB], [http://www.ebi.ac.uk/pdbsum/2e2s PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=2e2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e2s OCA], [https://pdbe.org/2e2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e2s RCSB], [https://www.ebi.ac.uk/pdbsum/2e2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e2s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TXAG_ALLOP TXAG_ALLOP]] Insect-selective toxin causing rapid but reversible paralysis in crickets. Suppresses the excitatory postsynaptic potentials evoked in lobster neuromuscular synaptic preparations, possibly by blocking the presynaptic calcium channel (Cav). Induces instantaneous reversible paralysis when injected into crickets.<ref>PMID:17644092</ref>
[https://www.uniprot.org/uniprot/TXAG_ALLOP TXAG_ALLOP] Insect-selective toxin causing rapid but reversible paralysis in crickets. Suppresses the excitatory postsynaptic potentials evoked in lobster neuromuscular synaptic preparations, possibly by blocking the presynaptic calcium channel (Cav). Induces instantaneous reversible paralysis when injected into crickets.<ref>PMID:17644092</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e2/2e2s_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e2/2e2s_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <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/chain_selection.php?pdb_ID=2ata 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=2e2s ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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</StructureSection>
</StructureSection>
[[Category: Allagelena opulenta]]
[[Category: Allagelena opulenta]]
[[Category: Yamaji, N]]
[[Category: Large Structures]]
[[Category: Cystine knot]]
[[Category: Yamaji N]]
[[Category: Presynaptic calcium channel inhibitor]]
[[Category: Toxin]]

Latest revision as of 10:56, 30 October 2024

Solution structure of agelenin, an insecticidal peptide from the venom of Agelena opulentaSolution structure of agelenin, an insecticidal peptide from the venom of Agelena opulenta

Structural highlights

2e2s is a 1 chain structure with sequence from Allagelena opulenta. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 20 models
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TXAG_ALLOP Insect-selective toxin causing rapid but reversible paralysis in crickets. Suppresses the excitatory postsynaptic potentials evoked in lobster neuromuscular synaptic preparations, possibly by blocking the presynaptic calcium channel (Cav). Induces instantaneous reversible paralysis when injected into crickets.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Agelenin, isolated from the Agelenidae spider Agelena opulenta, is a peptide composed of 35 amino acids. We determined the three-dimensional structure of agelenin using two-dimensional NMR spectroscopy. The structure is composed of a short antiparallel beta-sheet and four beta-turns, which are stabilized by three disulfide bonds. Agelenin has characteristic residues, Phe9, Ser28 and Arg33, which are arranged similarly to the pharmacophore of the insect channel inhibitor, omega-atracotoxin-Hv1a. These observations suggest that agelenin and omega-atracotoxin-Hv1a bind to insect calcium channels in a similar manner. We also suggest that another mode of action may operate in the channel inhibition by omega-agatoxin-IVA and omega-atracotoxin-Hv2a.

Solution structure of agelenin, an insecticidal peptide isolated from the spider Agelena opulenta, and its structural similarities to insect-specific calcium channel inhibitors.,Yamaji N, Sugase K, Nakajima T, Miki T, Wakamori M, Mori Y, Iwashita T FEBS Lett. 2007 Aug 7;581(20):3789-94. Epub 2007 Jul 10. PMID:17644092[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Yamaji N, Sugase K, Nakajima T, Miki T, Wakamori M, Mori Y, Iwashita T. Solution structure of agelenin, an insecticidal peptide isolated from the spider Agelena opulenta, and its structural similarities to insect-specific calcium channel inhibitors. FEBS Lett. 2007 Aug 7;581(20):3789-94. Epub 2007 Jul 10. PMID:17644092 doi:10.1016/j.febslet.2007.06.077
  2. Yamaji N, Sugase K, Nakajima T, Miki T, Wakamori M, Mori Y, Iwashita T. Solution structure of agelenin, an insecticidal peptide isolated from the spider Agelena opulenta, and its structural similarities to insect-specific calcium channel inhibitors. FEBS Lett. 2007 Aug 7;581(20):3789-94. Epub 2007 Jul 10. PMID:17644092 doi:10.1016/j.febslet.2007.06.077
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