1my0: Difference between revisions

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[[Image:1my0.jpg|left|200px]]
{{Seed}}
[[Image:1my0.png|left|200px]]


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{{STRUCTURE_1my0|  PDB=1my0  |  SCENE=  }}  
{{STRUCTURE_1my0|  PDB=1my0  |  SCENE=  }}  


'''crystal titration experiments (AMPA co-crystals soaked in 100 nM BrW)'''
===crystal titration experiments (AMPA co-crystals soaked in 100 nM BrW)===




==Overview==
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Numerous naturally occurring and synthetic alpha-amino acids act as agonists on (S)-2-amino-3-(3-hydroxy-5-methyl-4-isoxazole) propionic acid (AMPA) receptors but nevertheless display significant differences in their functional properties and modes of interaction. The 5-substituted willardiines are a series of compounds that exhibit a range of affinities, act as partial agonists, and give rise to intermediate levels of activation and desensitization. However, the molecular basis for the activities of 5-substituted willardiines has not been conclusively elaborated at the level of atomic resolution. Here we provide insight into the molecular basis of the potency and efficacy elicited by the 5-substituted willardiines on the basis of cocrystal structures with the GluR2 ligand-binding core. We also show that the crystallized ligand-binding core has an affinity for agonists similar to the ligand-binding core in solution. Analysis of multiple crystal lattices suggests modes by which the ligand-binding core dimers interact in the tetrameric receptor. These studies further our understanding of how subtle differences in the structures of agonists are correlated to changes in the conformation of residues and water molecules in the immediate binding pocket and to the degree of domain closure.
The line below this paragraph, {{ABSTRACT_PUBMED_12731861}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12731861 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12731861}}


==About this Structure==
==About this Structure==
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[[Category: Partial agonist]]
[[Category: Partial agonist]]
[[Category: S1s2]]
[[Category: S1s2]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:51:22 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:59:34 2008''

Revision as of 20:59, 27 July 2008

File:1my0.png

Template:STRUCTURE 1my0

crystal titration experiments (AMPA co-crystals soaked in 100 nM BrW)

Template:ABSTRACT PUBMED 12731861

About this Structure

1MY0 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Probing the function, conformational plasticity, and dimer-dimer contacts of the GluR2 ligand-binding core: studies of 5-substituted willardiines and GluR2 S1S2 in the crystal., Jin R, Gouaux E, Biochemistry. 2003 May 13;42(18):5201-13. PMID:12731861

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