1lmm
From Proteopedia
(New page: 200px<br /><applet load="1lmm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lmm" /> '''Solution Structure of Psmalmotoxin 1, the Fi...) |
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| - | [[Image:1lmm.gif|left|200px]]<br /><applet load="1lmm" size=" | + | [[Image:1lmm.gif|left|200px]]<br /><applet load="1lmm" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution Structure of Psmalmotoxin 1, the First Characterized Specific Blocker of ASIC1a NA+ channel'''<br /> | '''Solution Structure of Psmalmotoxin 1, the First Characterized Specific Blocker of ASIC1a NA+ channel'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Acid-sensing ion channels (ASICs) are thought to be important ion | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1LMM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Psalmopoeus_cambridgei Psalmopoeus cambridgei]. Full crystallographic information is available from [http:// | + | 1LMM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Psalmopoeus_cambridgei Psalmopoeus cambridgei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ick]] | [[Category: ick]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:20 2008'' |
Revision as of 11:46, 21 February 2008
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Solution Structure of Psmalmotoxin 1, the First Characterized Specific Blocker of ASIC1a NA+ channel
Overview
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.
About this Structure
1LMM is a Single protein structure of sequence from Psalmopoeus cambridgei. Full crystallographic information is available from OCA.
Reference
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
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