2e4x

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with 1S,3R-ACPD

Structural highlights

2e4x 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 2.75Å
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.

References

↑ 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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2e4x"

@@ Line 3: / Line 3: @@
 <StructureSection load='2e4x' size='340' side='right'caption='[[2e4x]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2e4x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E4X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E4X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2e4x]] 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=2E4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E4X FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C5B:(1S,3R)-1-AMINOCYCLOPENTANE-1,3-DICARBOXYLIC+ACID'>C5B</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2e4u|2e4u]], [[2e4v|2e4v]], [[2e4w|2e4w]], [[2e4y|2e4y]], [[2e4z|2e4z]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C5B:(1S,3R)-1-AMINOCYCLOPENTANE-1,3-DICARBOXYLIC+ACID'>C5B</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e4x OCA], [http://pdbe.org/2e4x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e4x RCSB], [http://www.ebi.ac.uk/pdbsum/2e4x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2e4x ProSAT]</span></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=2e4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e4x OCA], [https://pdbe.org/2e4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e4x RCSB], [https://www.ebi.ac.uk/pdbsum/2e4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e4x ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[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]]
@@ Line 15: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/2e4x_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 36: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
 [[Category: Large Structures]]
-[[Category: Jingami, H]]
+[[Category: Rattus norvegicus]]
-[[Category: Morikawa, K]]
+[[Category: Jingami H]]
-[[Category: Muto, T]]
+[[Category: Morikawa K]]
-[[Category: Tsuchiya, D]]
+[[Category: Muto T]]
-[[Category: Central nerve system]]
+[[Category: Tsuchiya D]]
-[[Category: G-protein-coupled receptor]]
-[[Category: Neuron]]
-[[Category: Signaling protein]]

2e4x

From Proteopedia

Current revision

Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with 1S,3R-ACPD

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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