View source for 1lmm


==Solution Structure of Psmalmotoxin 1, the First Characterized Specific Blocker of ASIC1a NA+ channel==
<StructureSection load='1lmm' size='340' side='right'caption='[[1lmm]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lmm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Psalmopoeus_cambridgei Psalmopoeus cambridgei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LMM 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=1lmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmm OCA], [https://pdbe.org/1lmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lmm RCSB], [https://www.ebi.ac.uk/pdbsum/1lmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lmm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TXP1_PSACA TXP1_PSACA] Potently and selectively blocks the acid-sensing ion channel ASIC1a/ACCN2. The blockade is rapid and reversible. Psalmotoxin 1 loses its capacity to block ASIC1a/ACCN2 as soon as this subunit is associated with another member of the family (ASIC2a/ACCN1 or ASIC3/ACCN3). The toxin can distinguish between the two ASIC1/ACCN2 splice variants ASIC1a/ACCN2 and ASIC1b/ACCN2.<ref>PMID:10829030</ref> 
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== Publication Abstract from PubMed ==
Acid-sensing ion channels (ASICs) are thought to be important ion channels, particularly for the perception of pain. Some of them may also contribute to synaptic plasticity, learning, and memory. Psalmotoxin 1 (PcTx1), the first potent and specific blocker of the ASIC1a proton-sensing channel, has been successfully expressed in the Drosophila melanogaster S2 cell recombinant expression system used here for the first time to produce a spider toxin. The recombinant toxin was identical in all respects to the native peptide, and its three-dimensional structure in solution was determined by means of (1)H 2D NMR spectroscopy. Surface characteristics of PcTx1 provide insights on key structural elements involved in the binding of PcTx1 to ASIC1a channels. They appear to be localized in the beta-sheet and the beta-turn linking the strands, as indicated by electrostatic anisotropy calculations, surface charge distribution, and the presence of residues known to be implicated in channel recognition by other inhibitor cystine knot (ICK) toxins.

Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton-gated cation channels.,Escoubas P, Bernard C, Lambeau G, Lazdunski M, Darbon H Protein Sci. 2003 Jul;12(7):1332-43. PMID:12824480<ref>PMID:12824480</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Psalmopoeus cambridgei]]
[[Category: Bernard C]]
[[Category: Darbon H]]
[[Category: Escoubas P]]
[[Category: Lazdunski M]]