Four residues of the extracellular N-terminal domain of the NR2A subunit control high-affinity Zn2 binding to NMDA receptors.Report as inadecuate




Four residues of the extracellular N-terminal domain of the NR2A subunit control high-affinity Zn2 binding to NMDA receptors. - Download this document for free, or read online. Document in PDF available to download.

1 NCM - Neurobiologie cellulaire et moléculaire 2 Istituto Cajal

Abstract : NMDA receptors are allosterically inhibited by Zn2+ ions in a voltage-independent manner. The apparent affinity for Zn2+ of the heteromeric NMDA receptors is determined by the subtype of NR2 subunit expressed, with NR2A-containing receptors being the most sensitive IC50, approximately 20 nM and NR2C-containing receptors being the least sensitive IC50, approximately 30 microM. Using chimeras constructed from these two NR2 subtypes, we show that the N-terminal LIVBP-like domain of the NR2A subunit controls the high-affinity Zn2+ inhibition. Mutations at four residues in this domain markedly reduce Zn2+ affinity by up to >500-fold without affecting either receptor activation by glutamate and glycine or inhibition by extracellular protons and Ni2+ ions, indicating that these residues most likely participate in high-affinity Zn2+ binding.





Author: A. Fayyazuddin - A. Villarroel - A. Le Goff - J. Lerma - J. Neyton -

Source: https://hal.archives-ouvertes.fr/



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