The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Selected cysteine residues in transmembrane domains of mu-opioid receptor are critical for effects of sulfhydryl reagents.

The effects of sulfhydryl-specific methanethiosulfonate (MTS) derivatives on mu-opioid receptor binding were examined in Chinese hamster ovary (CHO) cells that stably express mu-opioid receptors (HmuCHO). Three charged MTS derivatives inhibited the binding of [(3)H][D-Ala(2),N-MePhe(4),Gly-ol(5)]-enkephalin to mu-opioid receptors with IC(50) values ranging from 0.12 to 13 mM. Further characterization of the mu-opioid receptor interactions with ethylammonium MTS (the most potent among tested MTS reagents) revealed that ethylammonium MTS inhibition of ligand binding to the receptor was irreversible, with both the maximal receptor binding (B(max)) and the binding affinity (K(d)) being changed. Preincubation of HmuCHO cells with [D-Ala(2),N-MePhe(4), Gly-ol(5)]-enkephalin or naloxone prevented the receptor inactivation normally caused by MTS derivatives, indicating that the reactions may occur within or near the ligand-binding pocket on the receptor. To identify the susceptible sulfhydryl groups, each of the cysteine residues in the mu-receptor transmembrane domains were substituted with serine by site-directed mutagenesis. All of the mutant receptors transiently expressed in COS cells had receptor binding properties similar to the wild-type receptors. However, four mutant receptors with a serine substitution in transmembrane domain III (C161S), IV (C192S), V (C237S), or VII (C332S) displayed significant resistance against MTS inhibition compared with the wild-type receptor. We conclude that these four cysteine residues react with MTS reagents and are responsible for the effect of the MTS reagents on mu-opioid receptor binding.[1]


WikiGenes - Universities