Crystal Structures of the GluR5 and GluR6 Ligand Binding Cores: Molecular Mechanisms Underlying Kainate Receptor Selectivity
Until recently, our knowledge of neurotransmitter receptor biology came from anatomical, electrophysiological, and biochemical studies. Genome and cDNA sequencing projects have identified numerous receptor subtypes with distinct ligand binding properties. For example, 18 genes encode glutamate receptor ion channels. In this paper, Mark Mayer presents crystal structures of GluR5 and GluR6, two “kainate receptor” genes with close to 90% amino acid sequence identity, and reveals how unique functional properties are achieved via subtle changes in amino acid sequence. The results of such studies open the door for the development of subtype-specific ligands and are likely to play an emergent role in neurotransmitter receptor biology in the next decade.
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