Amyloid structure of high-order assembly of Leucine-rich amelogenin revealed by solid-state NMR
| Autor: | Jing Zhang, Junxia Lu, Cheng-Wei Ma, Dong X |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Magnetic Resonance Spectroscopy
Amyloid Amyloidogenic Proteins Matrix (biology) Microscopy Atomic Force Protein Structure Secondary Phosphates 03 medical and health sciences Mice stomatognathic system Microscopy Electron Transmission X-Ray Diffraction Structural Biology Leucine Animals Protein secondary structure 030304 developmental biology 0303 health sciences Viral matrix protein Enamel paint Amelogenin Chemistry 030302 biochemistry & molecular biology Hydrogen-Ion Concentration Recombinant Proteins Solid-state nuclear magnetic resonance visual_art Biophysics visual_art.visual_art_medium Calcium Self-assembly |
| Zdroj: | Journal of structural biology. 206(1) |
| ISSN: | 1095-8657 |
| Popis: | High-order assemblies of amelogenin, the major protein in enamel protein matrix, are believed to act as the template for enamel mineral formation. The Leucine-rich amelogenin (LRAP) is a natural splice-variant of amelogenin, a functional protein in vivo, containing conserved domains of amelogenin. In this work, we showed LRAP aggregates hierarchically into assemblies with various sizes including scattered beads, beads-on-a-string and gel-like precipitations in the presence of both calcium and phosphate ions. Solid-state NMR combined with X-ray diffraction and microscopic techniques, was applied to give a picture of LRAP self-assemblies at the atomic level. Our results, for the first time, confirmed LRAP assemblies with different sizes all contained a consistent rigid segment with β-sheet secondary structure (residues 12–27) and the β-sheet segment would further assemble into amyloid-like structures. |
| Databáze: | OpenAIRE |
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