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.

2i0b

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:21, 18 October 2017

Crystal structure of the GluR6 ligand binding core ELKQ mutant dimer at 1.96 Angstroms Resolution

Structural highlights

2i0b is a 3 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2f36, 1yae, 1lb8
Gene:	Grik2, Glur6 (Buffalo rat)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GRIK2_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. Modulates cell surface expression of NETO2 (By similarity).^[1] ^[2]

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

Desensitization is a universal feature of ligand-gated ion channels. Using the crystal structure of the GluR2 L483Y mutant channel as a guide, we attempted to build non-desensitizing kainate-subtype glutamate receptors. Success was achieved for GluR5, GluR6 and GluR7 with intermolecular disulfide cross-links but not by engineering the dimer interface. Crystallographic analysis of the GluR6 Y490C L752C dimer revealed relaxation from the active conformation, which functional studies reveal is not sufficient to trigger desensitization. The equivalent non-desensitizing cross-linked GluR2 mutant retained weak sensitivity to a positive allosteric modulator, which had no effect on GluR2 L483Y. These results establish that the active conformation of AMPA and kainate receptors is conserved and further show that their desensitization requires dimer rearrangements, that subtle structural differences account for their diverse functional properties and that the ligand-binding core dimer is a powerful regulator of ion-channel activity.

Conformational restriction blocks glutamate receptor desensitization.,Weston MC, Schuck P, Ghosal A, Rosenmund C, Mayer ML Nat Struct Mol Biol. 2006 Dec;13(12):1120-7. Epub 2006 Nov 19. PMID:17115050^[3]

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

References

↑ Martin S, Nishimune A, Mellor JR, Henley JM. SUMOylation regulates kainate-receptor-mediated synaptic transmission. Nature. 2007 May 17;447(7142):321-5. Epub 2007 May 7. PMID:17486098 doi:nature05736
↑ Weston MC, Schuck P, Ghosal A, Rosenmund C, Mayer ML. Conformational restriction blocks glutamate receptor desensitization. Nat Struct Mol Biol. 2006 Dec;13(12):1120-7. Epub 2006 Nov 19. PMID:17115050 doi:http://dx.doi.org/10.1038/nsmb1178
↑ Weston MC, Schuck P, Ghosal A, Rosenmund C, Mayer ML. Conformational restriction blocks glutamate receptor desensitization. Nat Struct Mol Biol. 2006 Dec;13(12):1120-7. Epub 2006 Nov 19. PMID:17115050 doi:http://dx.doi.org/10.1038/nsmb1178

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/2i0b"

Categories: Buffalo rat | Mayer, M L | Membrane protein

@@ Line 1: / Line 1: @@
 ==Crystal structure of the GluR6 ligand binding core ELKQ mutant dimer at 1.96 Angstroms Resolution==
 <StructureSection load='2i0b' size='340' side='right' caption='[[2i0b]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f36|2f36]], [[1yae|1yae]], [[1lb8|1lb8]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Grik2, Glur6 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i0b OCA], [http://pdbe.org/2i0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i0b RCSB], [http://www.ebi.ac.uk/pdbsum/2i0b 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=2i0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i0b OCA], [http://pdbe.org/2i0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i0b RCSB], [http://www.ebi.ac.uk/pdbsum/2i0b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2i0b ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 2i0b" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]]
 == References ==
 <references/>

2i0b

From Proteopedia

Revision as of 08:21, 18 October 2017

Crystal structure of the GluR6 ligand binding core ELKQ mutant dimer at 1.96 Angstroms Resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox