This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2ndb

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

NMR structure of omega-agatoxin IVA in DPC micelles

Structural highlights

2ndb is a 1 chain structure with sequence from Agelenopsis aperta. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

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^[8]

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

References

↑ Winterfield JR, Swartz KJ. A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels. J Gen Physiol. 2000 Nov;116(5):637-44. PMID:11055992
↑ Wang XH, Connor M, Wilson D, Wilson HI, Nicholson GM, Smith R, Shaw D, Mackay JP, Alewood PF, Christie MJ, King GF. Discovery and structure of a potent and highly specific blocker of insect calcium channels. J Biol Chem. 2001 Oct 26;276(43):40306-12. Epub 2001 Aug 24. PMID:11522785 doi:http://dx.doi.org/10.1074/jbc.M105206200
↑ Mintz IM, Venema VJ, Swiderek KM, Lee TD, Bean BP, Adams ME. P-type calcium channels blocked by the spider toxin omega-Aga-IVA. Nature. 1992 Feb 27;355(6363):827-9. PMID:1311418 doi:http://dx.doi.org/10.1038/355827a0
↑ Bickmeyer U, Rossler W, Wiegand H. Omega AGA toxin IVA blocks high-voltage-activated calcium channel currents in cultured pars intercerebralis neurosecretory cells of adult locusta migratoria. Neurosci Lett. 1994 Nov 7;181(1-2):113-6. PMID:7898748
↑ Nishio H, Kumagaye KY, Kubo S, Chen YN, Momiyama A, Takahashi T, Kimura T, Sakakibara S. Synthesis of omega-agatoxin IVA and its related peptides. Biochem Biophys Res Commun. 1993 Nov 15;196(3):1447-53. PMID:8250902 doi:http://dx.doi.org/10.1006/bbrc.1993.2414
↑ Wicher D, Penzlin H. Ca2+ currents in central insect neurons: electrophysiological and pharmacological properties. J Neurophysiol. 1997 Jan;77(1):186-99. PMID:9120560
↑ McDonough SI, Mintz IM, Bean BP. Alteration of P-type calcium channel gating by the spider toxin omega-Aga-IVA. Biophys J. 1997 May;72(5):2117-28. PMID:9129813 doi:http://dx.doi.org/10.1016/S0006-3495(97)78854-4
↑ Ryu JH, Jung HJ, Konishi S, Kim HH, Park ZY, Kim JI. Structure-activity relationships of omega-Agatoxin IVA in lipid membranes. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2016.11.025

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ndb"

Categories: Agelenopsis aperta | Large Structures | Kim JI | Ryu JH

@@ Line 1: / Line 1: @@
 ==NMR structure of omega-agatoxin IVA in DPC micelles==
-<StructureSection load='2ndb' size='340' side='right'caption='[[2ndb]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2ndb' size='340' side='right'caption='[[2ndb]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ndb]] is a 1 chain structure. 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>
+<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/TOG4A_AGEAP TOG4A_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:1311418</ref> <ref>PMID:8250902</ref> <ref>PMID:7898748</ref> <ref>PMID:9129813</ref> <ref>PMID:9120560</ref> <ref>PMID:11055992</ref> <ref>PMID:11522785</ref>
+[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 ==
@@ Line 21: / Line 21: @@
 __TOC__
 </StructureSection>
+[[Category: Agelenopsis aperta]]
 [[Category: Large Structures]]
-[[Category: Kim, J I]]
+[[Category: Kim JI]]
-[[Category: Ryu, J H]]
+[[Category: Ryu JH]]
-[[Category: Neurotoxin]]
-[[Category: Toxin]]

2ndb

From Proteopedia

Current revision

NMR structure of omega-agatoxin IVA in DPC micelles

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox