Cloned NMDA receptor channels of the NR1-NR2A, NR1-NR2B and NR1-NR2C t
ype show differences in argiotoxin636 block. Mutations of an asparagin
e residue located at a homologous position in the TM2 region of all NM
DA receptor subunits, which corresponds to the Q/R site of the AMPA re
ceptors, alters the argiotoxin636-induced block. The results suggest t
hat the toxin interacts at this amino acid position with the putative
pore forming TM2 region of the NMDA receptor subunits. Sequence differ
ences in the TM2 segment of NR2A and NR2C subunits are not responsible
for the subtype-specific sensitivity to argiotoxin636 as revealed by
site-directed mutagenesis.