These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Amyloid structure of high-order assembly of Leucine-rich amelogenin revealed by solid-state NMR.
    Author: Ma CW, Zhang J, Dong XQ, Lu JX.
    Journal: J Struct Biol; 2019 Apr 01; 206(1):29-35. PubMed ID: 29604451.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]