PMID:16787923

Citation	Rondard, P, Liu, J, Huang, S, Malhaire, F, Vol, C, Pinault, A, Labesse, G and Pin, JP (2006) Coupling of agonist binding to effector domain activation in metabotropic glutamate-like receptors. J. Biol. Chem. 281:24653-61
Abstract	Many membrane receptors are made of a ligand binding domain and an effector domain mediating intracellular signaling. This is the case for the metabotropic glutamate-like G-protein-coupled receptors. How ligand binding leads to the active conformation of the effector domain in such receptors is largely unknown. Here, we used an evolutionary trace analysis and mutagenesis to identify critical residues involved in the allosteric coupling between the Venus flytrap ligand binding domain (VFT) and the heptahelical G-protein activating domain of the metabotropic glutamate-like receptors. We have shown that a conserved interdomain disulfide bridge is required for this allosteric interaction. Taking into account that these receptors are homodimers, this finding provides important new information explaining how the different conformations of the dimer of VFT lead to different signaling of such dimeric receptors.
Links	PubMed Online version:10.1074/jbc.M602277200
Keywords	Animals; Binding Sites; Evolution, Molecular; Humans; Ligands; Models, Molecular; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Receptors, Metabotropic Glutamate/agonists; Receptors, Metabotropic Glutamate/chemistry; Receptors, Metabotropic Glutamate/metabolism
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

Useful Materials and Methods

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Annotations

<annotationlinks/>

EcoliWiki Links

Add links to pages that link here (e.g. gene, product, method pages)

References

See Help:References for how to manage references in EcoliWiki.