4ntx: Difference between revisions
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{{STRUCTURE_4ntx| PDB=4ntx | SCENE= }} | |||
===Structure of acid-sensing ion channel in complex with snake toxin and amiloride=== | |||
{{ABSTRACT_PUBMED_24507937}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/ASIC1_CHICK ASIC1_CHICK]] Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride (By similarity).<ref>PMID:16002453</ref> | |||
==About this Structure== | |||
[[4ntx]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NTX OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024507937</ref><references group="xtra"/><references/> | |||
[[Category: Baconguis, I.]] | |||
[[Category: Bohlen, C J.]] | |||
[[Category: Goehring, A.]] | |||
[[Category: Gouaux, E.]] | |||
[[Category: Julius, D.]] | |||
[[Category: Ion channel]] | |||
[[Category: Kunitz]] | |||
[[Category: Membrane]] | |||
[[Category: Nociception]] | |||
[[Category: Phospholipase a2-like]] | |||
[[Category: Transport protein-toxin complex]] |
Revision as of 20:18, 19 February 2014
Structure of acid-sensing ion channel in complex with snake toxin and amilorideStructure of acid-sensing ion channel in complex with snake toxin and amiloride
Template:ABSTRACT PUBMED 24507937
FunctionFunction
[ASIC1_CHICK] Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride (By similarity).[1]
About this StructureAbout this Structure
4ntx is a 3 chain structure. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Baconguis I, Bohlen CJ, Goehring A, Julius D, Gouaux E. X-ray structure of Acid-sensing ion channel 1-snake toxin complex reveals open state of a na(+)-selective channel. Cell. 2014 Feb 13;156(4):717-29. doi: 10.1016/j.cell.2014.01.011. Epub 2014 Feb, 6. PMID:24507937 doi:http://dx.doi.org/10.1016/j.cell.2014.01.011
- ↑ Coric T, Zheng D, Gerstein M, Canessa CM. Proton sensitivity of ASIC1 appeared with the rise of fishes by changes of residues in the region that follows TM1 in the ectodomain of the channel. J Physiol. 2005 Nov 1;568(Pt 3):725-35. Epub 2005 Jul 7. PMID:16002453 doi:http://dx.doi.org/jphysiol.2005.087734