4lml

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'''Unreleased structure'''
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{{STRUCTURE_4lml| PDB=4lml | SCENE= }}
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===GLIC double mutant I9'A T25'A===
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The entry 4lml is ON HOLD until Paper Publication
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==Function==
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[[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>
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Authors: Grosman, C., Gonzalez-Gutierrez, G.
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==About this Structure==
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[[4lml]] 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=4LML OCA].
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Description: GLIC double mutant I9'A T25'A
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Gloeobacter violaceus]]
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[[Category: Gonzalez-Gutierrez, G.]]
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[[Category: Grosman, C.]]
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[[Category: Membrane protein]]
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[[Category: Pentameric ligand-gated ion channel]]
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[[Category: Prokaryotic cys-loop receptor]]
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[[Category: Transport protein]]

Revision as of 09:53, 30 October 2013

Template:STRUCTURE 4lml

Contents

GLIC double mutant I9'A T25'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

4lml is a 5 chain structure with sequence from Gloeobacter violaceus. Full crystallographic information is available from OCA.

Reference

  1. ↑ 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

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