GRIN1 Protein, Human (C-His)

GRIN1, a pivotal component of NMDA receptor complexes, participates in the constitution of heterotetrameric ligand-gated ion channels that exhibit both high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation hinges on the intricate interplay of neurotransmitter binding, with glutamate binding to the epsilon subunit and glycine binding to the zeta subunit, combined with membrane depolarization to alleviate channel inhibition by Mg(2+). The sensitivity to glutamate, as well as the kinetics of the channel, is contingent upon the specific subunit composition. GRIN1 forms heterotetrameric channels typically comprised of two zeta subunits and two epsilon subunits, where the latter can be either GRIN2A, GRIN2B, GRIN2C, or GRIN2D. Additionally, it can participate in the formation of channels with GRIN3A or GRIN3B. The dynamic subunit composition in vivo further underscores the regulatory intricacies of GRIN1's involvement in NMDA receptor function. Furthermore, GRIN1 engages in various protein interactions, such as those with SNX27, DLG4, MPDZ, LRFN1, LRFN2, MYZAP, and PRR7, contributing to its multifaceted role within cellular processes.