1y20

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[[Image:1y20.gif|left|200px]]
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{{Seed}}
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[[Image:1y20.png|left|200px]]
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{{STRUCTURE_1y20| PDB=1y20 | SCENE= }}
{{STRUCTURE_1y20| PDB=1y20 | SCENE= }}
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'''Crystal structure of the NR1 ligand-binding core in complex with ACPC'''
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===Crystal structure of the NR1 ligand-binding core in complex with ACPC===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15996549}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15996549 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15996549}}
==About this Structure==
==About this Structure==
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[[Category: Ligand-binding complex]]
[[Category: Ligand-binding complex]]
[[Category: Protein-ligand complex]]
[[Category: Protein-ligand complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:47:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:21:07 2008''

Revision as of 12:21, 27 July 2008

Image:1y20.png

Template:STRUCTURE 1y20

Crystal structure of the NR1 ligand-binding core in complex with ACPC

Template:ABSTRACT PUBMED 15996549

About this Structure

1Y20 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Mechanism of partial agonist action at the NR1 subunit of NMDA receptors., Inanobe A, Furukawa H, Gouaux E, Neuron. 2005 Jul 7;47(1):71-84. PMID:15996549

Page seeded by OCA on Sun Jul 27 15:21:07 2008

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