Homologies and disparities of glutamate receptors: a critical analysis.
Based on analysis of aligned amino acid sequences the following statements are made: (i) There is evolutionary homology between the N-terminal extracellular region of ionotropic Glutamate receptors/Kainate Binding Proteins and a family of procaryote amino acid binding proteins. (ii) Homology of the N-terminal extracellular domain of the metabotropic glutamate receptors with a family of receptors with a guanylate cyclase intracellular domain appears to be valid. (iii) There is no evidence for homology between the N-terminal extracellular domain of the nicotinic Acetylcholine, GABA, Glycine and 5HT3 receptors and that of the ionotropic Glutamate receptors/Kainate Binding proteins. (iv) The proposal of homology for the N-terminal extracellular domain of metabotropic Glutamate receptors and that of ionotropic Glutamate receptors does not appear to hold.
Cockcroft
V B
VB
Biochemistry Department, Bath University, U.K.
Ortells
M O
MO
Thomas
P
P
Lunt
G G
GG
D000818:Animals; D005075:Biological Evolution; D006801:Humans; D008969:Molecular Sequence Data; D017470:Receptors, Glutamate / Q000235:genetics*; D018094:Receptors, Metabotropic Glutamate / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D017470:Receptors, Glutamate; D018094:Receptors, Metabotropic Glutamate