Article
Asn-265 of frog kainate binding protein is a functional glycosylation site: implications for the transmembrane topology of glutamate receptors.
FEBS letters - 17 Jul 1995
Wo Z G, Bian Z C, Oswald R E
Abstract excerpt
Kainate binding proteins (KBPs) from frog and goldfish brain are glycosylated, integral membrane proteins. These KBPs are homologous (35-40%) to the C-terminal half of AMPA and kainate receptors which have been shown to form glutamate-gated ion channels. We report here that the frog KBP has three functional N-glycosylation sites. Of particular interest, Asn-265, a residue located between two putative membrane...
Topics
- Amino Acid Sequence
- Animals
- Asparagine
- Base Sequence
- Cell Line
- Cell Membrane
- Glycosylation
- Hexosaminidases
- Humans
- Kainic Acid
- Microsomes
- Molecular Sequence Data