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2ndb
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR structure of omega-agatoxin IVA in DPC micelles== | |
| + | <StructureSection load='2ndb' size='340' side='right'caption='[[2ndb]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ndb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agelenopsis_aperta Agelenopsis aperta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NDB FirstGlance]. <br> | ||
| + | </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=2ndb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ndb OCA], [https://pdbe.org/2ndb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ndb RCSB], [https://www.ebi.ac.uk/pdbsum/2ndb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ndb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TX23A_AGEAP TX23A_AGEAP] Omega-agatoxins inhibit neuronal voltage-gated calcium channels. This toxin acts by modifying the gating of the high voltage activated P-type Cav2.1/CACNA1A channel. Is a potent blocker in both insect and mammalian central neurons.<ref>PMID:11055992</ref> <ref>PMID:11522785</ref> <ref>PMID:1311418</ref> <ref>PMID:7898748</ref> <ref>PMID:8250902</ref> <ref>PMID:9120560</ref> <ref>PMID:9129813</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | To analyze structural features of omega-Aga IVA, a gating modifier toxin from spider venom, we here investigated the NMR solution structure of omega-Aga IVA within DPC micelles. Under those conditions, the Cys-rich central region of omega-Aga IVA still retains the inhibitor Cys knot motif with three short antiparallel beta-strands seen in water. However, 15N HSQC spectra of omega-Aga IVA within micelles revealed that there are radical changes to the toxin's C-terminal tail and several loops upon binding to micelles. The C-terminal tail of omega-Aga IVA appears to assume a beta-turn like conformation within micelles, though it is disordered in water. Whole-cell patch clamp studies with several omega-Aga IVA analogs indicate that both the hydrophobic C-terminal tail and an Arg patch in the core region of omega-Aga IVA are critical for Cav2.1 blockade. These results suggest that the membrane environment stabilizes the structure of the toxin, enabling it to act in a manner similar to other gating modifier toxins, though its mode of interaction with the membrane and the channel is unique. | ||
| - | + | Structure-activity relationships of omega-Agatoxin IVA in lipid membranes.,Ryu JH, Jung HJ, Konishi S, Kim HH, Park ZY, Kim JI Biochem Biophys Res Commun. 2017 Jan 1;482(1):170-175. doi:, 10.1016/j.bbrc.2016.11.025. Epub 2016 Nov 9. PMID:27838299<ref>PMID:27838299</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Kim | + | <div class="pdbe-citations 2ndb" style="background-color:#fffaf0;"></div> |
| - | [[Category: Ryu | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Agelenopsis aperta]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kim JI]] | ||
| + | [[Category: Ryu JH]] | ||
Current revision
NMR structure of omega-agatoxin IVA in DPC micelles
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