2e4v: Difference between revisions

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[[Image:2e4v.gif|left|200px]]


{{Structure
==Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with DCG-IV==
|PDB= 2e4v |SIZE=350|CAPTION= <scene name='initialview01'>2e4v</scene>, resolution 2.4&Aring;
<StructureSection load='2e4v' size='340' side='right'caption='[[2e4v]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=2CG:(1R,2R)-3-[(S)-amino(carboxy)methyl]cyclopropane-1,2-dicarboxylic acid'>2CG</scene>
<table><tr><td colspan='2'>[[2e4v]] 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=2E4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E4V FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CG:(1R,2R)-3-[(S)-AMINO(CARBOXY)METHYL]CYCLOPROPANE-1,2-DICARBOXYLIC+ACID'>2CG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=2e4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e4v OCA], [https://pdbe.org/2e4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e4v RCSB], [https://www.ebi.ac.uk/pdbsum/2e4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e4v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GRM3_RAT GRM3_RAT] G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity.
== 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/e4/2e4v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2e4v ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metabotropic glutamate receptors play major roles in the activation of excitatory synapses in the central nerve system. We determined the crystal structure of the entire extracellular region of the group II receptor and that of the ligand-binding region of the group III receptor. A comparison among groups I, II, and III provides the structural basis that could account for the discrimination of group-specific agonists. Furthermore, the structure of group II includes the cysteine-rich domain, which is tightly linked to the ligand-binding domain by a disulfide bridge, suggesting a potential role in transmitting a ligand-induced conformational change into the downstream transmembrane region. The structure also reveals the lateral interaction between the two cysteine-rich domains, which could stimulate clustering of the dimeric receptors on the cell surface. We propose a general activation mechanism of the dimeric receptor coupled with both ligand-binding and interprotomer rearrangements.


'''Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with DCG-IV'''
Structures of the extracellular regions of the group II/III metabotropic glutamate receptors.,Muto T, Tsuchiya D, Morikawa K, Jingami H Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3759-64. Epub 2007 Feb 26. PMID:17360426<ref>PMID:17360426</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2e4v" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Metabotropic glutamate receptors play major roles in the activation of excitatory synapses in the central nerve system. We determined the crystal structure of the entire extracellular region of the group II receptor and that of the ligand-binding region of the group III receptor. A comparison among groups I, II, and III provides the structural basis that could account for the discrimination of group-specific agonists. Furthermore, the structure of group II includes the cysteine-rich domain, which is tightly linked to the ligand-binding domain by a disulfide bridge, suggesting a potential role in transmitting a ligand-induced conformational change into the downstream transmembrane region. The structure also reveals the lateral interaction between the two cysteine-rich domains, which could stimulate clustering of the dimeric receptors on the cell surface. We propose a general activation mechanism of the dimeric receptor coupled with both ligand-binding and interprotomer rearrangements.
*[[Metabotropic glutamate receptor 3D structures|Metabotropic glutamate receptor 3D structures]]
 
== References ==
==About this Structure==
<references/>
2E4V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E4V OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
Structures of the extracellular regions of the group II/III metabotropic glutamate receptors., Muto T, Tsuchiya D, Morikawa K, Jingami H, Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3759-64. Epub 2007 Feb 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17360426 17360426]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Jingami H]]
[[Category: Jingami, H.]]
[[Category: Morikawa K]]
[[Category: Morikawa, K.]]
[[Category: Muto T]]
[[Category: Muto, T.]]
[[Category: Tsuchiya D]]
[[Category: Tsuchiya, D.]]
[[Category: 2CG]]
[[Category: NAG]]
[[Category: central nerve system]]
[[Category: g-protein-coupled receptor]]
[[Category: neuron]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:35:20 2008''

Latest revision as of 12:05, 6 November 2024

Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with DCG-IVCrystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with DCG-IV

Structural highlights

2e4v 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 2.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GRM3_RAT G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity.

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

Metabotropic glutamate receptors play major roles in the activation of excitatory synapses in the central nerve system. We determined the crystal structure of the entire extracellular region of the group II receptor and that of the ligand-binding region of the group III receptor. A comparison among groups I, II, and III provides the structural basis that could account for the discrimination of group-specific agonists. Furthermore, the structure of group II includes the cysteine-rich domain, which is tightly linked to the ligand-binding domain by a disulfide bridge, suggesting a potential role in transmitting a ligand-induced conformational change into the downstream transmembrane region. The structure also reveals the lateral interaction between the two cysteine-rich domains, which could stimulate clustering of the dimeric receptors on the cell surface. We propose a general activation mechanism of the dimeric receptor coupled with both ligand-binding and interprotomer rearrangements.

Structures of the extracellular regions of the group II/III metabotropic glutamate receptors.,Muto T, Tsuchiya D, Morikawa K, Jingami H Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3759-64. Epub 2007 Feb 26. PMID:17360426[1]

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

See Also

References

  1. Muto T, Tsuchiya D, Morikawa K, Jingami H. Structures of the extracellular regions of the group II/III metabotropic glutamate receptors. Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3759-64. Epub 2007 Feb 26. PMID:17360426

2e4v, resolution 2.40Å

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