ID | 291 |
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Name | glycine receptors (protein family or complex) |
Synonyms | Glycine receptor; Glycine receptors |
ID | 336 |
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Name | strychnine |
CAS | strychnidin-10-one |
PubMed | Abstract | RScore(About this table) |
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8939452 | O'Connor V, Phelan PP, Fry JP: Interactions of and strychnine with their receptor recognition sites in mouse spinal cord. Behav Brain Res. 2007 Mar 12;178(1):70-81. Epub 2007 Jan 17. Interactions between the inhibitory neurotransmitter and its receptor antagonist strychnine have been studied in mouse spinal cord membranes and both agents employed to protect against residue selective protein modifying reagents in order to identify contact residues for ligand binding. was found to behave as a full competitive inhibitor of [3H]-strychnine binding, provided that precautions were taken to prevent radioligand binding to the glass-fibre filters used to terminate the assays. Hill coefficients for the inhibition of [3H]-strychnine binding were not significantly different from one, indicating a lack of cooperative interactions. For the protection experiments, N-bromosuccinimide, tetranitromethane, diethylpyrocarbonate and were used under conditions selective for and residues, respectively. Of these reagents, N-bromosuccinimide, tetranitromethane and diethylpyrocarbonate caused a decrease in total [3H]-strychnine binding without affecting the ability of unlabelled strychnine to compete. In contrast, the same reagents disrupted the ability of to inhibit [3H]-strychnine binding. The presence of either excess (10 (-2) M) or strychnine (10 (-4) M) during the above treatments was found to prevent the decrease in total and strychnine-specific [3H]-strychnine binding. However, only in the case of diethylpyrocarbonate treatment were both agonist and antagonist able to protect against the loss of -specific [3H]-strychnine binding. The reagent caused an increase in total and strychnine-specific [3H]-strychnine binding (which we have shown elsewhere to be at a site unrelated to the inhibitory glycine receptor). When the above protein modifying reagents were applied under the same conditions to specific strychnine binding antibodies, all four caused significant decreases in subsequent [3H]-strychnine binding. Strychnine was found to afford significant protection of the antibodies against N-bromosuccinimide, tetranitromethane and but not against diethylpyrocarbonate. Our results suggest that and strychnine compete at overlapping but conformationally distinct sites on the receptor. and residues are implicated as strychnine contact residues with a shared role for in the recognition of |
81(1,1,1,1) |