This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3h5v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:03, 16 March 2022) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3h5v.png|left|200px]]
 
-
<!--
+
==Crystal structure of the GluR2-ATD==
-
The line below this paragraph, containing "STRUCTURE_3h5v", creates the "Structure Box" on the page.
+
<StructureSection load='3h5v' size='340' side='right'caption='[[3h5v]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[3h5v]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H5V FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-
-->
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3h5w|3h5w]]</div></td></tr>
-
{{STRUCTURE_3h5v| PDB=3h5v | SCENE= }}
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Gria2, Glur2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3h5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h5v OCA], [https://pdbe.org/3h5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h5v RCSB], [https://www.ebi.ac.uk/pdbsum/3h5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h5v ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[[https://www.uniprot.org/uniprot/GRIA2_RAT GRIA2_RAT]] Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. 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. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.<ref>PMID:9351977</ref> <ref>PMID:19265014</ref> <ref>PMID:21172611</ref> <ref>PMID:12501192</ref> <ref>PMID:12015593</ref> <ref>PMID:12872125</ref> <ref>PMID:12730367</ref> <ref>PMID:16192394</ref> <ref>PMID:15591246</ref> <ref>PMID:17018279</ref> <ref>PMID:16483599</ref> <ref>PMID:19946266</ref> <ref>PMID:21317873</ref> <ref>PMID:21846932</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/h5/3h5v_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=3h5v ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Fast excitatory neurotransmission is mediated largely by ionotropic glutamate receptors (iGluRs), tetrameric, ligand-gated ion channel proteins comprised of three subfamilies, AMPA, kainate and NMDA receptors, with each subfamily sharing a common, modular-domain architecture. For all receptor subfamilies, active channels are exclusively formed by assemblages of subunits within the same subfamily, a molecular process principally encoded by the amino-terminal domain (ATD). However, the molecular basis by which the ATD guides subfamily-specific receptor assembly is not known. Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers and, by the analysis of crystal structures of the GluR2-ATD, propose mechanisms by which the ATD guides subfamily-specific receptor assembly.
-
===Crystal structure of the GluR2-ATD===
+
Crystal structure and association behaviour of the GluR2 amino-terminal domain.,Jin R, Singh SK, Gu S, Furukawa H, Sobolevsky AI, Zhou J, Jin Y, Gouaux E EMBO J. 2009 Jun 17;28(12):1812-23. Epub 2009 May 21. PMID:19461580<ref>PMID:19461580</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3h5v" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_19461580}}, adds the Publication Abstract to the page
+
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 19461580 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_19461580}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Buffalo rat]]
-
3H5V is a 3 chains structure of sequences 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=3H5V OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: Furukawa, H]]
-
==Reference==
+
[[Category: Gouaux, E]]
-
<ref group="xtra">PMID:19461580</ref><references group="xtra"/>
+
[[Category: Gu, S]]
-
[[Category: Rattus norvegicus]]
+
[[Category: Jin, R]]
-
[[Category: Furukawa, H.]]
+
[[Category: Jin, Y]]
-
[[Category: Gouaux, E.]]
+
[[Category: Singh, S K]]
-
[[Category: Gu, S.]]
+
[[Category: Sobolevsky, A]]
-
[[Category: Jin, R.]]
+
[[Category: Zhou, J]]
-
[[Category: Jin, Y.]]
+
-
[[Category: Singh, S K.]]
+
-
[[Category: Sobolevsky, A.]]
+
-
[[Category: Zhou, J.]]
+
-
[[Category: Alternative splicing]]
+
[[Category: Cell junction]]
[[Category: Cell junction]]
[[Category: Cell membrane]]
[[Category: Cell membrane]]
Line 53: Line 66:
[[Category: Transport]]
[[Category: Transport]]
[[Category: Transport protein]]
[[Category: Transport protein]]
- 
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 8 12:56:44 2009''
 

Current revision

Crystal structure of the GluR2-ATD

PDB ID 3h5v

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools