9c28
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of endogenous Glutamine synthetase from rat model of Alzheimer's disease== | |
| + | <StructureSection load='9c28' size='340' side='right'caption='[[9c28]], [[Resolution|resolution]] 3.12Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9c28]] is a 10 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=9C28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9C28 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]] 3.12Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=9c28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9c28 OCA], [https://pdbe.org/9c28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9c28 RCSB], [https://www.ebi.ac.uk/pdbsum/9c28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9c28 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GLNA_RAT GLNA_RAT] Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (PubMed:28323). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia (By similarity). Essential for proliferation of fetal skin fibroblasts. Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (By similarity). Plays a role in ribosomal 40S subunit biogenesis (By similarity). Through the interaction with BEST2, inhibits BEST2 channel activity by affecting the gating at the aperture in the absence of intracellular L-glutamate, but sensitizes BEST2 to intracellular L-glutamate, which promotes the opening of BEST2 and thus relieves its inhibitory effect on BEST2 (By similarity).[UniProtKB:P15104][UniProtKB:P15105]<ref>PMID:28323</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Studying native protein structures at near-atomic resolution in a crowded environment presents challenges. Consequently, understanding the structural intricacies of proteins within pathologically affected tissues often relies on mass spectrometry and proteomic analysis. Here, we utilized cryoelectron microscopy (cryo-EM) and the Build and Retrieve (BaR) method to investigate protein complexes' structural characteristics such as post-translational modification, active site occupancy, and arrested conformational state in Alzheimer's disease (AD) using brain lysate from a rat model (TgF344-AD). Our findings reveal novel insights into the architecture of these complexes, corroborated through mass spectrometry analysis. Interestingly, it has been shown that the dysfunction of these protein complexes extends beyond AD, implicating them in cancer, as well as other neurodegenerative disorders such as Parkinson's disease, Huntington's disease, and schizophrenia. By elucidating these structural details, our work not only enhances our understanding of disease pathology but also suggests new avenues for future approaches in therapeutic intervention. | ||
| - | + | Unveiling the structural proteome of an Alzheimer's disease rat brain model.,Samani EK, Hasan SMN, Waas M, Keszei AFA, Xu X, Heydari M, Hill ME, McLaurin J, Kislinger T, Mazhab-Jafari MT Structure. 2024 Nov 29:S0969-2126(24)00494-5. doi: 10.1016/j.str.2024.11.004. PMID:39615488<ref>PMID:39615488</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 9c28" style="background-color:#fffaf0;"></div> |
| - | [[Category: Khalili Samani | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rattus norvegicus]] | ||
| + | [[Category: Keszei AFA]] | ||
| + | [[Category: Khalili Samani E]] | ||
| + | [[Category: Mazhab-Jafari MT]] | ||
Current revision
Structure of endogenous Glutamine synthetase from rat model of Alzheimer's disease
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