2uxa: Difference between revisions

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==About this Structure==
==About this Structure==
2UXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GLU:'>GLU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn Binding Site For Residue A 1263'>AC1</scene>, <scene name='pdbsite=AC2:Zn Binding Site For Residue B 1262'>AC2</scene>, <scene name='pdbsite=AC3:Zn Binding Site For Residue C 1263'>AC3</scene>, <scene name='pdbsite=AC4:Zn Binding Site For Residue B 1263'>AC4</scene>, <scene name='pdbsite=AC5:Zn Binding Site For Residue C 1264'>AC5</scene>, <scene name='pdbsite=AC6:GLU Binding Site For Residue A 1264'>AC6</scene>, <scene name='pdbsite=AC7:GLU Binding Site For Residue C 1265'>AC7</scene> and <scene name='pdbsite=AC8:GLU Binding Site For Residue B 1264'>AC8</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UXA OCA].  
2UXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GLU:'>GLU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+1263'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+B+1262'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+C+1263'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Residue+B+1263'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Residue+C+1264'>AC5</scene>, <scene name='pdbsite=AC6:GLU+Binding+Site+For+Residue+A+1264'>AC6</scene>, <scene name='pdbsite=AC7:GLU+Binding+Site+For+Residue+C+1265'>AC7</scene> and <scene name='pdbsite=AC8:GLU+Binding+Site+For+Residue+B+1264'>AC8</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UXA OCA].  


==Reference==
==Reference==
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[[Category: transport]]
[[Category: transport]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 11:00:32 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:48:03 2008''

Revision as of 11:48, 3 February 2008

File:2uxa.gif


2uxa, resolution 2.38Å

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CRYSTAL STRUCTURE OF THE GLUR2-FLIP LIGAND BINDING DOMAIN, R/G UNEDITED.

OverviewOverview

The subunit composition determines AMPA receptor (AMPA-R) function and, trafficking. Mechanisms underlying channel assembly are thus central to, the efficacy and plasticity of glutamatergic synapses. We previously, showed that RNA editing at the Q/R site of the GluR2 subunit contributes, to the assembly of AMPA-R heteromers by attenuating formation of GluR2, homotetramers. Here we report that this function of the Q/R site depends, on subunit contacts between adjacent ligand binding domains (LBDs)., Changes of LBD interface contacts alter GluR2 assembly properties, forward, traffic, and expression at synapses. Interestingly, developmentally, regulated RNA editing within the LBD (at the R/G site) produces analogous, effects. Our data reveal that editing to glycine reduces the self-assembly, competence of this critical subunit and slows GluR2 maturation in the, endoplasmic reticulum (ER). Therefore, RNA editing sites, located at, strategic subunit interfaces, shape AMPA-R assembly and trafficking in a, developmentally regulated manner.

About this StructureAbout this Structure

2UXA is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Known structural/functional Sites: , , , , , , and . Full crystallographic information is available from OCA.

ReferenceReference

Developmentally regulated, combinatorial RNA processing modulates AMPA receptor biogenesis., Greger IH, Akamine P, Khatri L, Ziff EB, Neuron. 2006 Jul 6;51(1):85-97. PMID:16815334

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