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1wqk

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Revision as of 16:09, 11 April 2018

Solution structure of APETx1, a specific peptide inhibitor of human Ether-a-go-go-related gene potassium channels from the venom of the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin

Structural highlights

1wqk is a 1 chain structure with sequence from Anthopleura elegantissima. 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

[APT1_ANTEL] Potently and selectively blocks the HERG potassium voltage-gated channels KCNH2 (HERG1) KCNH6 (HERG2) and KCNH7 (HERG3). Acts by modifying the voltage dependence of the channel gating. Does not induce neurotoxic symptoms when injected into mice.^[1]

Publication Abstract from PubMed

APETx1 is a 42-amino acid toxin purified from the venom of the sea anemone Anthopleura elegantissima. This cysteine-rich peptide possesses three disulfide bridges (C4-C37, C6-C30, and C20-C38). Its pharmacological target is the Ether-a-gogo potassium channel. We herein determine the solution structure of APETx1 by use of conventional two-dimensional 1H-NMR techniques followed by torsion angle dynamics and refinement protocols. The calculated structure of APETx1 belongs to the disulfide-rich all-beta structural family, in which a three-stranded anti-parallel beta-sheet is the only secondary structure. APETx1 is the first Ether-a-gogo effector discovered to fold in this way. We therefore compare the structure of APETx1 to those of the two other known effectors of the Ether-a-gogo potassium channel, CnErg1 and BeKm-1, and analyze the topological disposition of key functional residues proposed by analysis of the electrostatic anisotropy. The interacting surface is made of a patch of aromatic residues (Y5, Y32, and F33) together with two basic residues (K8 and K18) at the periphery of the surface. We pinpoint the absence of the central lysine present in the functional surface of the two other Ether-a-gogo effectors.

Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin.,Chagot B, Diochot S, Pimentel C, Lazdunski M, Darbon H Proteins. 2005 May 1;59(2):380-6. PMID:15726634^[2]

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

References

↑ Diochot S, Loret E, Bruhn T, Beress L, Lazdunski M. APETx1, a new toxin from the sea anemone Anthopleura elegantissima, blocks voltage-gated human ether-a-go-go-related gene potassium channels. Mol Pharmacol. 2003 Jul;64(1):59-69. PMID:12815161 doi:http://dx.doi.org/10.1124/mol.64.1.59
↑ Chagot B, Diochot S, Pimentel C, Lazdunski M, Darbon H. Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin. Proteins. 2005 May 1;59(2):380-6. PMID:15726634 doi:10.1002/prot.20425

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/1wqk"

@@ Line 1: / Line 1: @@
 ==Solution structure of APETx1, a specific peptide inhibitor of human Ether-a-go-go-related gene potassium channels from the venom of the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin==
 <StructureSection load='1wqk' size='340' side='right' caption='[[1wqk]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1wqk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anthopleura_elegantissima Anthopleura elegantissima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WQK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WQK FirstGlance]. <br>
-</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=1wqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wqk OCA], [http://pdbe.org/1wqk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wqk RCSB], [http://www.ebi.ac.uk/pdbsum/1wqk PDBsum]</span></td></tr>
+</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=1wqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wqk OCA], [http://pdbe.org/1wqk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wqk RCSB], [http://www.ebi.ac.uk/pdbsum/1wqk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wqk ProSAT]</span></td></tr>
 </table>
 == Function ==

1wqk

From Proteopedia

Revision as of 16:09, 11 April 2018

Solution structure of APETx1, a specific peptide inhibitor of human Ether-a-go-go-related gene potassium channels from the venom of the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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