Proper receptor signalling in a mutant catfish gonadotropin-releasing hormone receptor lacking the highly conserved Asp(90) residue

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...

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Published inFEBS letters Vol. 501; no. 2-3; p. 131
Main Authors Blomenröhr, M, Kühne, R, Hund, E, Leurs, R, Bogerd, J, ter Laak, T
Format Journal Article
LanguageEnglish
Published England 20.07.2001
Subjects
Animals
Aspartic Acid - genetics
Binding Sites
Catfishes
Conserved Sequence
Gonadotropin-Releasing Hormone - metabolism
Humans
Inositol Phosphates - metabolism
Lysine - genetics
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Protein Structure, Tertiary
Receptors, LHRH - chemistry
Receptors, LHRH - genetics
Receptors, LHRH - metabolism
Signal Transduction - physiology
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Summary: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 Asp(90) of the catfish GnRH receptor can be substituted by a neutral Asn(90) without abolishing receptor signalling if another negatively charged Glu(93) is introduced in a proximal region of the receptor interior, thereby mimicking the Glu(90)-Lys(121) salt bridge of mammalian GnRH receptors.
ISSN:0014-5793
DOI:10.1016/S0014-5793(01)02647-3