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1wxn

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Revision as of 16:17, 11 April 2018

Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels

Structural highlights

1wxn 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

[APT2_ANTEL] Potently and selectively blocks the acid-sensing ion channel ASIC3 (ACCN3). The blockade is rapid and reversible. Also inhibits heteromeric ASIC2b-ASIC3 (ACCN1-ACCN3) channel, while it has less affinity for ASIC1b-ASIC3 (ACCN2-ACCN3), ASIC1a-ASIC3 (ACCN2-ASIC3).^[1]

Publication Abstract from PubMed

Acid-sensing ion channels (ASIC) are proton-gated sodium channels that have been implicated in pain transduction associated with acidosis in inflamed or ischemic tissues. APETx2, a peptide toxin effector of ASIC3, has been purified from an extract of the sea anemone Anthopleura elegantissima. APETx2 is a 42-amino-acid peptide cross-linked by three disulfide bridges. Its three-dimensional structure, as determined by conventional two-dimensional 1H-NMR, consists of a compact disulfide-bonded core composed of a four-stranded beta-sheet. It belongs to the disulfide-rich all-beta structural family encompassing peptide toxins commonly found in animal venoms. The structural characteristics of APETx2 are compared with that of PcTx1, another effector of ASIC channels but specific to the ASIC1a subtype and to APETx1, a toxin structurally related to APETx2, which targets the HERG potassium channel. Structural comparisons, coupled with the analysis of the electrostatic characteristics of these various ion channel effectors, led us to suggest a putative channel interaction surface for APETx2, encompassing its N terminus together with the type I-beta turn connecting beta-strands III and IV. This basic surface (R31 and R17) is also rich in aromatic residues (Y16, F15, Y32, and F33). An additional region made of the type II'-beta turn connecting beta-strands I and II could also play a role in the specificity observed for these different ion effectors.

Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels.,Chagot B, Escoubas P, Diochot S, Bernard C, Lazdunski M, Darbon H Protein Sci. 2005 Aug;14(8):2003-10. Epub 2005 Jun 29. PMID:15987885^[2]

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

References

↑ Diochot S, Baron A, Rash LD, Deval E, Escoubas P, Scarzello S, Salinas M, Lazdunski M. A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid-sensitive channel in sensory neurons. EMBO J. 2004 Apr 7;23(7):1516-25. Epub 2004 Mar 25. PMID:15044953 doi:http://dx.doi.org/10.1038/sj.emboj.7600177
↑ Chagot B, Escoubas P, Diochot S, Bernard C, Lazdunski M, Darbon H. Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels. Protein Sci. 2005 Aug;14(8):2003-10. Epub 2005 Jun 29. PMID:15987885 doi:ps.051378905

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/1wxn"

@@ Line 1: / Line 1: @@
 ==Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels==
 <StructureSection load='1wxn' size='340' side='right' caption='[[1wxn]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1wxn]] 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=1WXN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WXN 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=1wxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wxn OCA], [http://pdbe.org/1wxn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wxn RCSB], [http://www.ebi.ac.uk/pdbsum/1wxn 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=1wxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wxn OCA], [http://pdbe.org/1wxn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wxn RCSB], [http://www.ebi.ac.uk/pdbsum/1wxn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wxn ProSAT]</span></td></tr>
 </table>
 == Function ==

1wxn

From Proteopedia

Revision as of 16:17, 11 April 2018

Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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