GLIC

The GLIC receptor is a bacterial (Gloeobacter) Ligand-gated Ion Channel, homolog to the nicotinic acetylcholine receptors. It is a proton-gated, cation-selective channel, and like the nicotinic acetylcholine receptors is a functional pentameric oligomer. However while its eukaryotic homologues are hetero-oligomeric, all until now known bactria known to express LICs encode a single monomeric unit, indicating the GLIC to be functionally homo-oligomeric.[1]

The similarity of amino-acid sequence to the eukaryotic LGICs is not localized to any single or particular tertiary domain, indicating the similar function of the GLIC to its eukaryotic equivalents. Regardless, the purpose of regulating the threshold for action potential excitation in the nerve signal transmission of multicellular organisms cannot translate to single-cell organisms, thereby not making the purpose of bacterial LGICs immediately obvious.

Structure

The structure of the open channel structure was solved by two independent research teams in 2009[2][3] at low pH values of 4-4.6 (GLIC being proton-gated).

See also

References

  1. Tasneem A, Iyer L, Jakobsson E, Aravind L (2004). "Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels". Genome Biology. 6 (1): R4. doi:10.1186/gb-2004-6-1-r4. ISSN 1465-6906. PMC 549065Freely accessible. PMID 15642096.
  2. Bocquet N, Nury H, Baaden M, Le Poupon C, Changeux JP, Delarue M, Corringer PJ (2009). "X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation". Nature. 457: 111–114. doi:10.1038/nature07462. ISSN 0028-0836.
  3. Hilf RJ, Dutzler R (2009). "Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel". Nature. 457: 115–U122. doi:10.1038/nature07461. ISSN 0028-0836.

External links


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