Proper receptor signalling in a mutant catfish gonadotropin‐releasing hormone receptor lacking the highly conserved Asp90 residue

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Abstract
The negatively charged side chain of an Asp residue in transmembrane domain 2 is likely to play an important role in receptor signalling since it is highly conserved in the whole family of G protein‐coupled receptors, except in mammalian gonadotropin‐releasing hormone (GnRH) receptors. In this paper we show that the conserved Asp90 of the catfish GnRH receptor can be substituted by a neutral Asn90 without abolishing receptor signalling if another negatively charged Glu93 is introduced in a proximal region of the receptor interior, thereby mimicking the Glu90–Lys121 salt bridge of mammalian GnRH receptors.