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3c36

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Revision as of 08:17, 25 October 2017

Crystal structure of GluR5 ligand-binding core in complex with ammonium ions at 1.68 Angstrom resolution

Structural highlights

3c36 is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1tt1, 2pbw, 2ojt, 2f34, 3c31, 3c32, 3c33, 3c34, 3c35
Gene:	GRIK1, GLUR5 (Rattus norvegicus)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GRIK1_RAT] Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Membrane proteins function in a polarized ionic environment with sodium-rich extracellular and potassium-rich intracellular solutions. Glutamate receptors that mediate excitatory synaptic transmission in the brain show unusual sensitivity to external ions, resulting in an apparent requirement for sodium in order for glutamate to activate kainate receptors. Here, we solve the structure of the Na(+)-binding sites and determine the mechanism by which allosteric anions and cations regulate ligand-binding dimer stability, and hence the rate of desensitization and receptor availability for gating by glutamate. We establish a stoichiometry for binding of 2 Na(+) to 1 Cl(-) and show that allosteric anions and cations bind at physically discrete sites with strong electric fields, that the binding sites are not saturated in CSF, and that the requirement of kainate receptors for Na(+) occurs simply because other cations bind with lower affinity and have lower efficacy compared to Na(+).

Molecular basis of kainate receptor modulation by sodium.,Plested AJ, Vijayan R, Biggin PC, Mayer ML Neuron. 2008 Jun 12;58(5):720-35. PMID:18549784^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mayer ML, Ghosal A, Dolman NP, Jane DE. Crystal structures of the kainate receptor GluR5 ligand binding core dimer with novel GluR5-selective antagonists. J Neurosci. 2006 Mar 15;26(11):2852-61. PMID:16540562 doi:26/11/2852
↑ Plested AJ, Vijayan R, Biggin PC, Mayer ML. Molecular basis of kainate receptor modulation by sodium. Neuron. 2008 Jun 12;58(5):720-35. PMID:18549784 doi:10.1016/j.neuron.2008.04.001

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3c36"

Categories: Rattus norvegicus | Mayer, M L | Membrane protein

@@ Line 1: / Line 1: @@
 ==Crystal structure of GluR5 ligand-binding core in complex with ammonium ions at 1.68 Angstrom resolution==
 <StructureSection load='3c36' size='340' side='right' caption='[[3c36]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tt1|1tt1]], [[2pbw|2pbw]], [[2ojt|2ojt]], [[2f34|2f34]], [[3c31|3c31]], [[3c32|3c32]], [[3c33|3c33]], [[3c34|3c34]], [[3c35|3c35]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRIK1, GLUR5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c36 OCA], [http://pdbe.org/3c36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c36 RCSB], [http://www.ebi.ac.uk/pdbsum/3c36 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c36 OCA], [http://pdbe.org/3c36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c36 RCSB], [http://www.ebi.ac.uk/pdbsum/3c36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c36 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 3c36" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]]
 == References ==
 <references/>

3c36

From Proteopedia

Revision as of 08:17, 25 October 2017

Crystal structure of GluR5 ligand-binding core in complex with ammonium ions at 1.68 Angstrom resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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