2ojt: Difference between revisions

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New page: left|200px<br /><applet load="2ojt" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ojt, resolution 1.95Å" /> '''Structure and mechan...
 
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[[Image:2ojt.jpg|left|200px]]<br /><applet load="2ojt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ojt, resolution 1.95&Aring;" />
'''Structure and mechanism of kainate receptor modulation by anions'''<br />


==Overview==
==Structure and mechanism of kainate receptor modulation by anions==
L-glutamate, the major excitatory neurotransmitter in the human brain, activates a family of ligand-gated ion channels, the major subtypes of, which are named AMPA, kainate, and NMDA receptors. In common with many, signal transduction proteins, glutamate receptors are modulated by ions, and small molecules, including Ca(2+), Mg(2+), Zn(2+), protons, polyamines, and steroids. Strikingly, the activation of kainate receptors, by glutamate requires the presence of both Na(+) and Cl(-) in the, extracellular solution, and in the absence of these ions, receptor, activity is abolished. Here, we identify the site and mechanism of action, of anions. Surprisingly, we find that Cl(-) ions are essential structural, components of kainate receptors. Cl(-) ions bind in a cavity formed at the, interface between subunits in a dimer pair. In the absence of Cl(-), dimer, stability is reduced, the rate of desensitization increases, and the, fraction of receptors competent for activation by glutamate drops, precipitously.
<StructureSection load='2ojt' size='340' side='right'caption='[[2ojt]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ojt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OJT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=UBA:(S)-1-(2-AMINO-2-CARBOXYETHYL)-3(2-CARBOXYTHIOPHENE-3-YL-METHYL)-5-METHYLPYRIMIDINE-2,4-DIONE'>UBA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ojt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ojt OCA], [https://pdbe.org/2ojt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ojt RCSB], [https://www.ebi.ac.uk/pdbsum/2ojt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ojt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GRIK1_RAT 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.<ref>PMID:16540562</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oj/2ojt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ojt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
L-glutamate, the major excitatory neurotransmitter in the human brain, activates a family of ligand-gated ion channels, the major subtypes of which are named AMPA, kainate, and NMDA receptors. In common with many signal transduction proteins, glutamate receptors are modulated by ions and small molecules, including Ca(2+), Mg(2+), Zn(2+), protons, polyamines, and steroids. Strikingly, the activation of kainate receptors by glutamate requires the presence of both Na(+) and Cl(-) in the extracellular solution, and in the absence of these ions, receptor activity is abolished. Here, we identify the site and mechanism of action of anions. Surprisingly, we find that Cl(-) ions are essential structural components of kainate receptors. Cl(-) ions bind in a cavity formed at the interface between subunits in a dimer pair. In the absence of Cl(-), dimer stability is reduced, the rate of desensitization increases, and the fraction of receptors competent for activation by glutamate drops precipitously.


==About this Structure==
Structure and mechanism of kainate receptor modulation by anions.,Plested AJ, Mayer ML Neuron. 2007 Mar 15;53(6):829-41. PMID:17359918<ref>PMID:17359918</ref>
2OJT 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=BR:'>BR</scene>, <scene name='pdbligand=1PE:'>1PE</scene> and <scene name='pdbligand=UBA:'>UBA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OJT OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure and mechanism of kainate receptor modulation by anions., Plested AJ, Mayer ML, Neuron. 2007 Mar 15;53(6):829-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17359918 17359918]
</div>
<div class="pdbe-citations 2ojt" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Mayer ML]]
[[Category: Mayer, M.L.]]
[[Category: 1PE]]
[[Category: BR]]
[[Category: UBA]]
[[Category: membrane protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:12:08 2008''

Latest revision as of 13:41, 30 August 2023

Structure and mechanism of kainate receptor modulation by anionsStructure and mechanism of kainate receptor modulation by anions

Structural highlights

2ojt 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.
Method:X-ray diffraction, Resolution 1.95Å
Ligands:, ,
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

L-glutamate, the major excitatory neurotransmitter in the human brain, activates a family of ligand-gated ion channels, the major subtypes of which are named AMPA, kainate, and NMDA receptors. In common with many signal transduction proteins, glutamate receptors are modulated by ions and small molecules, including Ca(2+), Mg(2+), Zn(2+), protons, polyamines, and steroids. Strikingly, the activation of kainate receptors by glutamate requires the presence of both Na(+) and Cl(-) in the extracellular solution, and in the absence of these ions, receptor activity is abolished. Here, we identify the site and mechanism of action of anions. Surprisingly, we find that Cl(-) ions are essential structural components of kainate receptors. Cl(-) ions bind in a cavity formed at the interface between subunits in a dimer pair. In the absence of Cl(-), dimer stability is reduced, the rate of desensitization increases, and the fraction of receptors competent for activation by glutamate drops precipitously.

Structure and mechanism of kainate receptor modulation by anions.,Plested AJ, Mayer ML Neuron. 2007 Mar 15;53(6):829-41. PMID:17359918[2]

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

See Also

References

  1. 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
  2. Plested AJ, Mayer ML. Structure and mechanism of kainate receptor modulation by anions. Neuron. 2007 Mar 15;53(6):829-41. PMID:17359918 doi:10.1016/j.neuron.2007.02.025

2ojt, resolution 1.95Å

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