A point mutation within the coding sequence of the primary subunit of
the N-methyl-D-asparlate (NMDA) subtype of glutamate receptor (glutami
ne substitution for histidine at position 780) exhibits a higher affin
ity for NMDA than the wild type receptor (EC(50) 5 versus 27 mu M). To
our knowledge this is the first point mutation of this ligand-gated i
on channel described with higher agonist affinity. This observation ma
y help further localize the agonist binding site and help to understan
d the heterogeneity of agonist affinity within the glutamate receptor
family.