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KBP  -  kainate binding protein

Gallus gallus

 
 
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High impact information on LOC396300

  • This raises the possibility, that kainate binding protein may form part of an ion channel and may be a subunit of a kainate subtype of glutamate receptor [1].
  • As a result, we present here the subsets of amino acids accounting for the binding free energies and specificities of KBP for kainate, glutamate, and CNQX and propose a three-dimensional model, at the microarchitectural level, of the glutamatergic binding domain [2].
  • Accordingly, we propose that the glycine-rich motif of KBP forms part of a guanine nucleotide binding site [3].
  • Site-directed mutagenesis of residues K72 and Y73 within the glycine-rich motif followed by the expression of the KBP mutants at the surface of HEK 293 cells showed a decrease in GTP binding affinity by factors of 10 and 100 respectively [3].
  • Here, we report that guanine, but not adenine, nucleotides interact with KBP by inhibiting [3H]KA binding in a competitive-like manner, displaying IC50 values in the micromolar range [3].
 

Biological context of LOC396300

 

Anatomical context of LOC396300

  • Membranes prepared from the culture cells displayed, using 25 nM [3H]kainate, the binding of 4.1 pmol of [3H]kainate/mg protein and showed the presence in Western blots of the two polypeptides of 49 and 93 kDa attributed to the kainate binding protein [6].
  • In this study, we have analysed the anatomical and subcellular distribution of the alpha-amino-3-hydroxyl-5-methyl-isoxazole-4-propionate receptors in the rat hippocampus and cerebellum, using a monoclonal antibody that was raised against a kainate binding protein purified from frog brain [7].
  • The association of Bergmann glial processes, carrying the Mr = 49,000 kainate binding protein, with the Purkinje cell dendrites and spine synapses could provide a basis for neuronal signalling to the Bergmann glia, possibly by glutamate [8].
 

Associations of LOC396300 with chemical compounds

References

  1. Molecular structure of the chick cerebellar kainate-binding subunit of a putative glutamate receptor. Gregor, P., Mano, I., Maoz, I., McKeown, M., Teichberg, V.I. Nature (1989) [Pubmed]
  2. Identification of the amino acid subsets accounting for the ligand binding specificity of a glutamate receptor. Paas, Y., Eisenstein, M., Medevielle, F., Teichberg, V.I., Devillers-Thiéry, A. Neuron (1996) [Pubmed]
  3. Identification of an extracellular motif involved in the binding of guanine nucleotides by a glutamate receptor. Paas, Y., Devillers-Thiéry, A., Changeux, J.P., Medevielle, F., Teichberg, V.I. EMBO J. (1996) [Pubmed]
  4. Kainate binding proteins possess functional ion channel domains. Villmann, C., Bull, L., Hollmann, M. J. Neurosci. (1997) [Pubmed]
  5. Glutamate-dependent transcriptional regulation of the chkbp gene: signaling mechanisms. Aguirre, A., López-Bayghen, E., Ortega, A. J. Neurosci. Res. (2002) [Pubmed]
  6. Properties of kainate receptor/channels on cultured Bergmann glia. Ortega, A., Eshhar, N., Teichberg, V.I. Neuroscience (1991) [Pubmed]
  7. Localization of AMPA receptors in the hippocampus and cerebellum of the rat using an anti-receptor monoclonal antibody. Hampson, D.R., Huang, X.P., Oberdorfer, M.D., Goh, J.W., Auyeung, A., Wenthold, R.J. Neuroscience (1992) [Pubmed]
  8. Subcellular localization of a putative kainate receptor in Bergmann glial cells using a monoclonal antibody in the chick and fish cerebellar cortex. Somogyi, P., Eshhar, N., Teichberg, V.I., Roberts, J.D. Neuroscience (1990) [Pubmed]
  9. Transcriptional regulation through glutamate receptors: Involvement of tyrosine kinases. López-Bayghen, E., Aguirre, A., Ortega, A. J. Neurosci. Res. (2003) [Pubmed]
 
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