[NMR paper] Amyloid Structure of High-order Assembly of Leucine-Rich Amelogenin Revealed by Solid-state NMR.

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Amyloid Structure of High-order Assembly of Leucine-Rich Amelogenin Revealed by Solid-state NMR.

Related Articles Amyloid Structure of High-order Assembly of Leucine-Rich Amelogenin Revealed by Solid-state NMR.

J Struct Biol. 2018 Mar 28;:

Authors: Ma CW, Zhang J, Dong XQ, Lu JX

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 ?-sheet secondary structure (residues 12-27) and the ?-sheet segment would further assemble into amyloid-like structures.


PMID: 29604451 [PubMed - as supplied by publisher]



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