9s41: Difference between revisions

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'''Unreleased structure'''


The entry 9s41 is ON HOLD
==Cerebellar GluA1/4 TMD with TARP gamma 7 (focused refinement)==
<StructureSection load='9s41' size='340' side='right'caption='[[9s41]], [[Resolution|resolution]] 3.66&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9s41]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9S41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9S41 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.66&#8491;</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=9s41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9s41 OCA], [https://pdbe.org/9s41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9s41 RCSB], [https://www.ebi.ac.uk/pdbsum/9s41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9s41 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A286ZS63_PIG A0A286ZS63_PIG] Receptor for glutamate that functions as a 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.[RuleBase:RU367118]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
AMPA receptors (AMPARs) are multimodal transducers of glutamatergic signals throughout the brain. Their diversity is exemplified in the cerebellum; at afferent synapses, AMPARs mediate high-frequency excitation, whereas in Bergmann glia (BG) they support calcium transients that modulate synaptic transmission. This spectrum arises from different combinations of core subunits (GluA1-4), auxiliary proteins, and post-transcriptional modifications. Here, using mass-spectrometry, cryo-EM, and electrophysiology, we characterize major cerebellar AMPARs in pig: calcium-impermeable GluA2/A4 heteromers with four TARP subunits, mainly neuronal in origin, and BG-specific calcium-permeable GluA1/A4 heteromers containing two Type-2 TARPs. We also showed that GluA4 receptors consistently exhibit compact N-terminal domains that promote their synaptic delivery. Our study defines the organizational principles of mammalian cerebellar AMPAR complexes and reveals how different receptor subtypes support cell-type specific functions.


Authors:  
Structure and organization of AMPA receptor-TARP complexes in the mammalian cerebellum.,Scrutton AM, Sengupta N, Ivica J, Stockwell I, Peak-Chew S, Singh B, Suzuki K, Chang VT, McLaughlin SH, Krieger JM, Aricescu AR, Greger IH Science. 2025 Dec 11:eaeb3577. doi: 10.1126/science.aeb3577. PMID:41379938<ref>PMID:41379938</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9s41" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Greger IH]]
[[Category: Krieger JM]]
[[Category: Scrutton A]]
[[Category: Sengupta N]]

Latest revision as of 05:26, 24 December 2025

Cerebellar GluA1/4 TMD with TARP gamma 7 (focused refinement)

9s41, resolution 3.66Å

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