4ntw: Difference between revisions
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==Structure of acid-sensing ion channel in complex with snake toxin== | ==Structure of acid-sensing ion channel in complex with snake toxin== | ||
<StructureSection load='4ntw' size='340' side='right' caption='[[4ntw]], [[Resolution|resolution]] 2.07Å' scene=''> | <StructureSection load='4ntw' size='340' side='right' caption='[[4ntw]], [[Resolution|resolution]] 2.07Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hgc|3hgc]], [[2qts|2qts]], [[4nyk|4nyk]], [[4ntx|4ntx]], [[4nty|4nty]], [[4fz0|4fz0]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hgc|3hgc]], [[2qts|2qts]], [[4nyk|4nyk]], [[4ntx|4ntx]], [[4nty|4nty]], [[4fz0|4fz0]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASIC1, ACCN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASIC1, ACCN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=4ntw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ntw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ntw RCSB], [http://www.ebi.ac.uk/pdbsum/4ntw PDBsum]</span></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=4ntw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ntw OCA], [http://pdbe.org/4ntw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ntw RCSB], [http://www.ebi.ac.uk/pdbsum/4ntw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ntw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ntw" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels|Ion channels]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 22:29, 5 August 2016
Structure of acid-sensing ion channel in complex with snake toxinStructure of acid-sensing ion channel in complex with snake toxin
Structural highlights
Function[ASIC1_CHICK] Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride (By similarity).[1] Publication Abstract from PubMedAcid-sensing ion channels (ASICs) detect extracellular protons produced during inflammation or ischemic injury and belong to the superfamily of degenerin/epithelial sodium channels. Here, we determine the cocrystal structure of chicken ASIC1a with MitTx, a pain-inducing toxin from the Texas coral snake, to define the structure of the open state of ASIC1a. In the MitTx-bound open state and in the previously determined low-pH desensitized state, TM2 is a discontinuous alpha helix in which the Gly-Ala-Ser selectivity filter adopts an extended, belt-like conformation, swapping the cytoplasmic one-third of TM2 with an adjacent subunit. Gly 443 residues of the selectivity filter provide a ring of three carbonyl oxygen atoms with a radius of approximately 3.6 A, presenting an energetic barrier for hydrated ions. The ASIC1a-MitTx complex illuminates the mechanism of MitTx action, defines the structure of the selectivity filter of voltage-independent, sodium-selective ion channels, and captures the open state of an ASIC. X-ray structure of Acid-sensing ion channel 1-snake toxin complex reveals open state of a na(+)-selective channel.,Baconguis I, Bohlen CJ, Goehring A, Julius D, Gouaux E Cell. 2014 Feb 13;156(4):717-29. doi: 10.1016/j.cell.2014.01.011. Epub 2014 Feb, 6. PMID:24507937[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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