This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1mxv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mxv.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1mxv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mxv| PDB=1mxv | SCENE= }}
{{STRUCTURE_1mxv| PDB=1mxv | SCENE= }}
-
'''crystal titration experiments (AMPA co-crystals soaked in 10 mM BrW)'''
+
===crystal titration experiments (AMPA co-crystals soaked in 10 mM BrW)===
-
==Overview==
+
<!--
-
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.
 +
-->
 +
{{ABSTRACT_PUBMED_12731861}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Partial agonist]]
[[Category: Partial agonist]]
[[Category: S1s2]]
[[Category: S1s2]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:51:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:48:30 2008''

Revision as of 08:48, 28 July 2008

Image:1mxv.png

Template:STRUCTURE 1mxv

crystal titration experiments (AMPA co-crystals soaked in 10 mM BrW)

Template:ABSTRACT PUBMED 12731861

About this Structure

1MXV 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

Page seeded by OCA on Mon Jul 28 11:48:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mxv"
Personal tools