4lmk: Difference between revisions
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' | {{STRUCTURE_4lmk| PDB=4lmk | SCENE= }} | ||
===GLIC Liganded-closed-channel Conformation, Mutant Y27'A=== | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/GLIC_GLOVI GLIC_GLOVI]] Cationic channel with similar permeabilities for Na(+) and K(+), that is activated by an increase of the proton concentration on the extracellular side. Displays no permeability for chloride ions. Shows slow kinetics of activation, no desensitization and a single channel conductance of 8 pS. Might contribute to adaptation to external pH change.<ref>PMID:17167423</ref> | |||
==About this Structure== | |||
[[4lmk]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Gloeobacter_violaceus Gloeobacter violaceus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LMK OCA]. | |||
==Reference== | |||
<references group="xtra"/><references/> | |||
[[Category: Gloeobacter violaceus]] | |||
[[Category: Gonzalez-Gutierrez, G.]] | |||
[[Category: Grosman, C.]] | |||
[[Category: Membrane protein]] | |||
[[Category: Pentameric ligand-gated ion channel]] | |||
[[Category: Prokaryotic cys-loop receptor]] | |||
[[Category: Transport protein]] | |||
Revision as of 09:53, 30 October 2013
GLIC Liganded-closed-channel Conformation, Mutant Y27'A
Function
[GLIC_GLOVI] Cationic channel with similar permeabilities for Na(+) and K(+), that is activated by an increase of the proton concentration on the extracellular side. Displays no permeability for chloride ions. Shows slow kinetics of activation, no desensitization and a single channel conductance of 8 pS. Might contribute to adaptation to external pH change.[1]
About this Structure
4lmk is a 5 chain structure with sequence from Gloeobacter violaceus. Full crystallographic information is available from OCA.
Reference
- ↑ Bocquet N, Prado de Carvalho L, Cartaud J, Neyton J, Le Poupon C, Taly A, Grutter T, Changeux JP, Corringer PJ. A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family. Nature. 2007 Jan 4;445(7123):116-9. Epub 2006 Dec 10. PMID:17167423 doi:10.1038/nature05371
