Summary
In order to elucidate the amino acid residues that are involved in binding of somatostatin-14 (SST-14), mutations were introduced into the cDNA encoding somatostatin receptor subtype 3 (SSTR 3) using a polymerase chain reaction(PCR-)based approach. A glutamate residue (E92) in the transmembrane domain II of the SSTR3 sequence was subsequently mutated into a valine residue (E92V) referred to the sequence of SSTR5, which is known to preferentially bind SST-28. The mutation showed no significant differences in agonist binding, but caused enhancement of the sodium sensitivity of the receptor-agonist interaction.
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© 1996 Birkhäuser Verlag Basel/Switzerland
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Nehring, R.B., Meyerhof, W., Richter, D. (1996). Reduction of somatostatin-14 binding to the rat somatostatin receptor subtype 3 by Na+ is enhanced by mutation of the glutamate residue 92 in the transmembrane domain II. In: Krisch, B., Mentlein, R. (eds) The Peptidergic Neuron. Advances in Life Sciences. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-9010-6_14
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DOI: https://doi.org/10.1007/978-3-0348-9010-6_14
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