2ndb: Difference between revisions

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'''Unreleased structure'''


The entry 2ndb is ON HOLD  until Paper Publication
==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='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'>[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.


Authors: Ryu,, J., Kim, J.
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>


Description: NMR structure of omega-agatoxin IVA in DPC micelles
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Kim, J]]
<div class="pdbe-citations 2ndb" style="background-color:#fffaf0;"></div>
[[Category: Ryu,, J]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Agelenopsis aperta]]
[[Category: Large Structures]]
[[Category: Kim JI]]
[[Category: Ryu JH]]
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