9C28
Structure of endogenous Glutamine synthetase from rat model of Alzheimer's disease
Summary for 9C28
| Entry DOI | 10.2210/pdb9c28/pdb |
| Related | 9C21 |
| EMDB information | 45137 |
| Descriptor | Glutamine synthetase, MANGANESE (II) ION (2 entities in total) |
| Functional Keywords | glutamine synthetase, ligase |
| Biological source | Rattus norvegicus (Norway rat) |
| Total number of polymer chains | 10 |
| Total formula weight | 424336.53 |
| Authors | Khalili Samani, E.,Keszei, A.F.A.,Mazhab-Jafari, M.T. (deposition date: 2024-05-30, release date: 2024-12-11) |
| Primary citation | Samani, E.K.,Hasan, S.M.N.,Waas, M.,Keszei, A.F.A.,Xu, X.,Heydari, M.,Hill, M.E.,McLaurin, J.,Kislinger, T.,Mazhab-Jafari, M.T. Unveiling the structural proteome of an Alzheimer's disease rat brain model. Structure, 2024 Cited by PubMed Abstract: 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. PubMed: 39615488DOI: 10.1016/j.str.2024.11.004 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.12 Å) |
Structure validation
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