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© Structural Dynamics Of Macromolecules
The structure of a bacterial analog of the nicotinic receptor (one color per subunit) inserted into the cell membrane (grey and orange). A representation of the volume accessible to ions is shown in yellow.
Publication : Structure (London, England : 1993)

Structure and pharmacology of pentameric receptor channels: from bacteria to brain

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Structure (London, England : 1993) - 06 Jun 2012

Corringer PJ, Poitevin F, Prevost MS, Sauguet L, Delarue M, Changeux JP

Link to Pubmed [PMID] – 22681900

Structure 2012 Jun;20(6):941-56

Orthologs of the pentameric receptor channels that mediate fast synaptic transmission in the central and peripheral nervous systems have been found in several bacterial species and in a single archaea genus. Recent X-ray structures of bacterial and invertebrate pentameric receptors point to a striking conservation of the structural features within the whole family, even between distant prokaryotic and eukaryotic members. These structural data reveal general principles of molecular organization that allow allosteric membrane proteins to mediate chemoelectric transduction. Notably, several conformations have been solved, including open and closed channels with distinct global tertiary and quaternary structure. The data reveal features of the ion channel architecture and of diverse categories of binding sites, such as those that bind orthosteric ligands, including neurotransmitters, and those that bind allosteric modulators, such as general anesthetics, ivermectin, or lipids. In this review, we summarize the most recent data, discuss insights into the mechanism of action in these systems, and elaborate on newly opened avenues for drug design.

https://www.ncbi.nlm.nih.gov/pubmed/22681900