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| pubmed-article:15996549 | lifeskim:mentions | umls-concept:C0243192 | lld:lifeskim |
| pubmed-article:15996549 | lifeskim:mentions | umls-concept:C0080093 | lld:lifeskim |
| pubmed-article:15996549 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
| pubmed-article:15996549 | lifeskim:mentions | umls-concept:C1538051 | lld:lifeskim |
| pubmed-article:15996549 | lifeskim:mentions | umls-concept:C0728938 | lld:lifeskim |
| pubmed-article:15996549 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:15996549 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:15996549 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15996549 | pubmed:dateCreated | 2005-7-5 | lld:pubmed |
| pubmed-article:15996549 | pubmed:abstractText | Partial agonists produce submaximal activation of ligand-gated ion channels. To address the question of partial agonist action at the NR1 subunit of the NMDA receptor, we performed crystallographic and electrophysiological studies with 1-aminocyclopropane-1-carboxylic acid (ACPC), 1-aminocyclobutane-1-carboxylic acid (ACBC), and 1-aminocyclopentane-1-carboxylic acid (cycloleucine), three compounds with incrementally larger carbocyclic rings. Whereas ACPC and ACBC partially activate the NMDA receptor by 80% and 42%, respectively, their cocrystal structures of the NR1 ligand binding core show the same degree of domain closure as found in the complex with glycine, a full agonist, illustrating that the NR1 subunit provides a new paradigm for partial agonist action that is distinct from that of the evolutionarily related GluR2, AMPA-sensitive receptor. Cycloleucine behaves as an antagonist and stabilizes an open-cleft conformation. The NR1-cycloleucine complex forms a dimer that is similar to the GluR2 dimer, thereby suggesting a conserved mode of subunit-subunit interaction in AMPA and NMDA receptors. | lld:pubmed |
| pubmed-article:15996549 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15996549 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15996549 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15996549 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15996549 | pubmed:issn | 0896-6273 | lld:pubmed |
| pubmed-article:15996549 | pubmed:author | pubmed-author:GouauxEricE | lld:pubmed |
| pubmed-article:15996549 | pubmed:author | pubmed-author:InanobeAtsush... | lld:pubmed |
| pubmed-article:15996549 | pubmed:author | pubmed-author:FurukawaHiroy... | lld:pubmed |
| pubmed-article:15996549 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15996549 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:15996549 | pubmed:volume | 47 | lld:pubmed |
| pubmed-article:15996549 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15996549 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15996549 | pubmed:pagination | 71-84 | lld:pubmed |
| pubmed-article:15996549 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15996549 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15996549 | pubmed:articleTitle | Mechanism of partial agonist action at the NR1 subunit of NMDA receptors. | lld:pubmed |
| pubmed-article:15996549 | pubmed:affiliation | Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA. | lld:pubmed |
| pubmed-article:15996549 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15996549 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15996549 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:15996549 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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