Molecular organization of a zinc binding n-terminal modulatory domain in a NMDA receptor subunit. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Neuron Année : 2000

Molecular organization of a zinc binding n-terminal modulatory domain in a NMDA receptor subunit.

Résumé

Ionotropic glutamate receptors (iGluRs) bind agonists in a domain that has been crystallized and shown to have a bilobed structure. Eukaryotic iGluRs also possess a second extracellular N-terminal domain related to the bacterial periplasmic binding protein LIVBP. In NMDA receptors, the high-affinity Zn inhibition is eliminated by mutations in the LIVBP-like domain of the NR2A subunit. Using LIVBP structure, we have modeled this domain as two lobes connected by a hinge and show that six residues controlling Zn inhibition form two clusters facing each other across a central cleft. Upon Zn binding the two lobes close tightly around the divalent cation. Thus, the extracellular region of NR2A consists of a tandem of Venus flytrap domains, one binding the agonist and the other a modulatory ligand. Such a functional organization may apply to other eukaryotic iGluRs.
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Dates et versions

hal-00139991 , version 1 (04-04-2007)

Identifiants

  • HAL Id : hal-00139991 , version 1
  • PUBMED : 11163276

Citer

P. Paoletti, F. Perin-Dureau, A. Fayyazuddin, A. Le Goff, I. Callebaut, et al.. Molecular organization of a zinc binding n-terminal modulatory domain in a NMDA receptor subunit.. Neuron, 2000, 28 (3), pp.911-25. ⟨hal-00139991⟩
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