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.

5kc8

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of the amino-terminal domain (ATD) of iGluR Delta-2 (GluD2)

Structural highlights

5kc8 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.751Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

GRID2_HUMAN Autosomal recessive congenital cerebellar ataxia due to GRID2 deficiency. The disease is caused by mutations affecting the gene represented in this entry.

Function

GRID2_HUMAN Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists.

Publication Abstract from PubMed

Ionotropic glutamate receptor (iGluR) family members are integrated into supramolecular complexes that modulate their location and function at excitatory synapses. However, a lack of structural information beyond isolated receptors or fragments thereof currently limits the mechanistic understanding of physiological iGluR signaling. Here, we report structural and functional analyses of the prototypical molecular bridge linking postsynaptic iGluR delta2 (GluD2) and presynaptic beta-neurexin 1 (beta-NRX1) via Cbln1, a C1q-like synaptic organizer. We show how Cbln1 hexamers "anchor" GluD2 amino-terminal domain dimers to monomeric beta-NRX1. This arrangement promotes synaptogenesis and is essential for D: -serine-dependent GluD2 signaling in vivo, which underlies long-term depression of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses and motor coordination in developing mice. These results lead to a model where protein and small-molecule ligands synergistically control synaptic iGluR function.

Structural basis for integration of GluD receptors within synaptic organizer complexes.,Elegheert J, Kakegawa W, Clay JE, Shanks NF, Behiels E, Matsuda K, Kohda K, Miura E, Rossmann M, Mitakidis N, Motohashi J, Chang VT, Siebold C, Greger IH, Nakagawa T, Yuzaki M, Aricescu AR Science. 2016 Jul 15;353(6296):295-9. doi: 10.1126/science.aae0104. PMID:27418511^[1]

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

References

↑ Elegheert J, Kakegawa W, Clay JE, Shanks NF, Behiels E, Matsuda K, Kohda K, Miura E, Rossmann M, Mitakidis N, Motohashi J, Chang VT, Siebold C, Greger IH, Nakagawa T, Yuzaki M, Aricescu AR. Structural basis for integration of GluD receptors within synaptic organizer complexes. Science. 2016 Jul 15;353(6296):295-9. doi: 10.1126/science.aae0104. PMID:27418511 doi:http://dx.doi.org/10.1126/science.aae0104

1 Structural highlights
2 Disease
3 Function
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/5kc8"

@@ Line 3: / Line 3: @@
 <StructureSection load='5kc8' size='340' side='right'caption='[[5kc8]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5kc8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KC8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KC8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5kc8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KC8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.751&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRID2, GLURD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5kc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kc8 OCA], [http://pdbe.org/5kc8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kc8 RCSB], [http://www.ebi.ac.uk/pdbsum/5kc8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kc8 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=5kc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kc8 OCA], [https://pdbe.org/5kc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kc8 RCSB], [https://www.ebi.ac.uk/pdbsum/5kc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kc8 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/GRID2_HUMAN GRID2_HUMAN]] Autosomal recessive congenital cerebellar ataxia due to GRID2 deficiency. The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/GRID2_HUMAN GRID2_HUMAN] Autosomal recessive congenital cerebellar ataxia due to GRID2 deficiency. The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/GRID2_HUMAN GRID2_HUMAN]] Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists.
+[https://www.uniprot.org/uniprot/GRID2_HUMAN GRID2_HUMAN] Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 28: / Line 28: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Aricescu, A R]]
+[[Category: Aricescu AR]]
-[[Category: Clay, J E]]
+[[Category: Clay JE]]
-[[Category: Elegheert, J]]
+[[Category: Elegheert J]]
-[[Category: Siebold, C]]
+[[Category: Siebold C]]
-[[Category: Neurotransmission]]
-[[Category: Signaling protein]]

5kc8

From Proteopedia

Current revision

Crystal structure of the amino-terminal domain (ATD) of iGluR Delta-2 (GluD2)

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox