1wxn
From Proteopedia
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'''Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels''' | '''Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels''' | ||
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[[Category: Escoubas, P.]] | [[Category: Escoubas, P.]] | ||
[[Category: Lazdunski, M.]] | [[Category: Lazdunski, M.]] | ||
| - | [[Category: | + | [[Category: Acid-sensing ion channel]] |
| - | [[Category: | + | [[Category: Anthopleura elegantissima toxin 2]] |
| - | [[Category: | + | [[Category: Apetx2]] |
| - | [[Category: | + | [[Category: Asic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:16:26 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 11:16, 3 May 2008
Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels
Overview
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.
About this Structure
1WXN is a Single protein structure of sequence from Anthopleura elegantissima. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 14:16:26 2008
