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Yorodumi- EMDB-65957: Cryo-EM map of hIAPP fibrils extracted from a donor with T2D and ... -
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Basic information
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| Title | Cryo-EM map of hIAPP fibrils extracted from a donor with T2D and Intraductal Papillary Mucinous Neoplasm | |||||||||
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Keywords | Amyloid fibrils / type II diabetes / hIAPP / PROTEIN FIBRIL | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 3.42 Å | |||||||||
Authors | Cao Q / Liu W | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Cell / Year: 2026Title: Structure of pancreatic hIAPP fibrils derived from patients with type 2 diabetes. Authors: Wenjing Liu / Jianting Han / Wei Gong / Fei Zhang / Qin Cao / ![]() Abstract: Type 2 diabetes (T2D) impacts the quality of life and lifespan of nearly 10% of the global population. Human islet amyloid polypeptide (hIAPP) constitutes a major component of islet amyloid ...Type 2 diabetes (T2D) impacts the quality of life and lifespan of nearly 10% of the global population. Human islet amyloid polypeptide (hIAPP) constitutes a major component of islet amyloid deposition in patients with T2D, with hIAPP fibrils believed to play a key role in the pathogenesis of T2D. In this study, we determined the cryo-electron microscopy (cryo-EM) structure of hIAPP fibrils extracted from surgically resected pancreases of three donors with T2D. These fibrils exhibit a uniform morphology, comprising two symmetrical protofilaments encompassing residues 2-37 of hIAPP and adopting an Ω-shaped fold. The structure of pancreatic hIAPP fibrils differs from that of fibrils formed in vitro. Additional densities were observed in the pancreatic hIAPP fibrils, suggesting ligand binding that may play significant roles in the pathogenesis of T2D. Collectively, our study presents the atomic structure of pathological hIAPP fibrils, contributing to the therapeutic and mechanistic exploration of T2D. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_65957.map.gz | 11.9 MB | EMDB map data format | |
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| Header (meta data) | emd-65957-v30.xml emd-65957.xml | 14.7 KB 14.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_65957_fsc.xml | 12.8 KB | Display | FSC data file |
| Images | emd_65957.png | 34.4 KB | ||
| Filedesc metadata | emd-65957.cif.gz | 4.4 KB | ||
| Others | emd_65957_half_map_1.map.gz emd_65957_half_map_2.map.gz | 11.9 MB 11.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-65957 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-65957 | HTTPS FTP |
-Validation report
| Summary document | emd_65957_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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| Full document | emd_65957_full_validation.pdf.gz | 1 MB | Display | |
| Data in XML | emd_65957_validation.xml.gz | 15.4 KB | Display | |
| Data in CIF | emd_65957_validation.cif.gz | 20.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-65957 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-65957 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_65957.map.gz / Format: CCP4 / Size: 12.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.932 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_65957_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_65957_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : hIAPP fibrils
| Entire | Name: hIAPP fibrils |
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| Components |
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-Supramolecule #1: hIAPP fibrils
| Supramolecule | Name: hIAPP fibrils / type: tissue / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Islet amyloid polypeptide
| Macromolecule | Name: Islet amyloid polypeptide / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Sequence | String: KCNTATCATQ RLANFLVHSS NNFGAILSST NVGSNTY |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | helical reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK II |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
China, 1 items
Citation


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Processing
FIELD EMISSION GUN

