Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1999-8-2
pubmed:abstractText
N-Methyl-D-aspartate receptor channels are composed of an NR1 subunit and at least one of the NR2 subunits (NR2A-D). Activation of the N-methyl-d-aspartate receptor requires the co-agonists glycine and glutamate. It has been proposed that the NR1 subunit possesses a glycine-binding site. We have expressed a soluble form of the NR1 subunit, which was produced by connecting the N-terminal extracellular region with the extracellular loop between the third and fourth membrane segments, by a baculovirus system along with full-length and truncated membrane-bound forms. The soluble NR1 receptor was efficiently secreted into the culture medium and showed a high affinity for ligands. The Kd of a glycine-site antagonist, [3H]MDL 105,519 [(E)-3-(2-phenyl-2-carboxyethenyl)-4, 6-dichloro-1H-indole-2-carboxylic acid], for the soluble receptor was 3.89+/-0.97 nM, which was comparable to the Kd of 4.47+/-1.39 nM for the membrane-bound full-length form. These values were close to the values reported previously with the use of rat brain membranes and Chinese hamster ovary cells expressing the full-length form of the NR1 subunit. The Ki values of other glycine-site antagonists, L-689,560 (trans-2-carboxy-5,7-dichloro - 4 - phenylaminocarbonylamino - 1,2,3,4 - tetrahydroquinoline), 5, 7-dichlorokynurenate and 5,7-dinitroquinoxaline-2,3-dione, for the soluble receptor were also similar to those for the full-length form of NR1. [3H]MDL 105,519 binding was also inhibited by the agonists glycine and d-serine. Thus the affinity and selectivity of ligand-binding characteristics of the NR1 subunit is conferred on the soluble form of the NR1 subunit. This soluble receptor provides a good experimental tool for initiating a biophysical analysis of the N-methyl-d-aspartate receptor channel protein.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-1350383, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-1374164, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-1699567, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-1834949, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-2155495, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-2433595, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-2904680, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-7527641, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-7857646, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-7870047, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-7919785, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-7993626, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-8011339, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-8210177, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-8382885, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-8428958, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-8557052, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-8785317, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-8858976, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-8861200, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-8894619, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-9115742, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-9425000, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-9526012, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-9582347, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-9685327, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-9760184, http://linkedlifedata.com/resource/pubmed/commentcorrection/10359652-9804426
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
340 ( Pt 3)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
687-92
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:10359652-Amidohydrolases, pubmed-meshheading:10359652-Aminoquinolines, pubmed-meshheading:10359652-Animals, pubmed-meshheading:10359652-Baculoviridae, pubmed-meshheading:10359652-Binding Sites, pubmed-meshheading:10359652-Blotting, Western, pubmed-meshheading:10359652-Cell Line, pubmed-meshheading:10359652-Genetic Vectors, pubmed-meshheading:10359652-Glycine, pubmed-meshheading:10359652-Glycosylation, pubmed-meshheading:10359652-Indoles, pubmed-meshheading:10359652-Inhibitory Concentration 50, pubmed-meshheading:10359652-Insects, pubmed-meshheading:10359652-Ligands, pubmed-meshheading:10359652-Molecular Weight, pubmed-meshheading:10359652-Peptide Fragments, pubmed-meshheading:10359652-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, pubmed-meshheading:10359652-Receptors, N-Methyl-D-Aspartate, pubmed-meshheading:10359652-Recombinant Fusion Proteins, pubmed-meshheading:10359652-Solubility
pubmed:year
1999
pubmed:articleTitle
Expression and characterization of a glycine-binding fragment of the N-methyl-D-aspartate receptor subunit NR1.
pubmed:affiliation
Department of Molecular Biology, Biomolecular Engineering Research Institute (BERI), 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan.
pubmed:publicationType
Journal Article