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Figure 2. — Microglia, Trem2, and Neurodegeneration.
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Created: 2026-04-21T18:29:40
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ID: paper-fig-paper-486e714f1641-2
Figure 2.Figure 2
Domain structure of the Trem2 protein and its association with Alzheimer disease (AD) risk. ( A ) Human Trem2 protein domain structure: this schematic illustrates the structural domains of the human Trem2 protein, including the signal peptide (SP), transmembrane domain (TM), and C-terminal tail (CT). Notable are the common variants associated with AD risk and the cleavage sites for ADAM17/10, which are crucial for Trem2’s functional modulation in the disease context. ( B ) Membrane-bound three-dimensional (3D) structure of Trem2-DAP12 complex: derived from AlphaFold (ID: Q9NZC2 ), this representation showcases the 3D conformation of Trem2 as it anchors to the cell membrane through a transmembrane helix. TREM2’s interaction with DAP12 (AlphaFold ID: O43914 ) is highlighted, showing electrostatic interactions (involving lysine and arginine residues) within the transmembrane domains. Additionally, the dimerization of two DAP12 proteins through a disulfide bond is depicted, emphasizing t
▸Metadata
| pmid | paper-486e714f1641 |
| caption | Domain structure of the Trem2 protein and its association with Alzheimer disease (AD) risk. ( A ) Human Trem2 protein domain structure: this schematic illustrates the structural domains of the human T |
| image_url | https://www.ebi.ac.uk/europepmc/articles/PMC11576490/bin/10.1177_10738584241254118-fig2.jpg |
| paper_title | Microglia, Trem2, and Neurodegeneration. |
| figure_label | Figure 2. |
| figure_number | 2 |
| _schema_version | 1 |
| source_strategy | pmc_api |
📊 Evidence Profile
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