Intrinsically disordered proteins drive enamel formation via an evolutionarily conserved self-assembly motif

• DOI: 10.1073/pnas.1615334114
• Publication Date: 2017-02-15T01:35:19Z
• Authors: Tomas Wald; Frantisek Spoutil; Adriana Osickova; Michaela Prochazkova; Oldrich Benada; Petr Kasparek; Ladislav Bumba; Ophir D. Klein; Radislav Sedlacek; Peter Sebo; Jan Prochazka; Radim Osicka
• Keywords: Amelogenin; Mineralized tissues; Matrix (chemical analysis)

Significance Formation of the hardest mineralized tissue in vertebrates, tooth enamel, relies on a unique set enamel matrix proteins (EMPs). These EMPs assemble into 3D extracellular organic that directs deposition calcium and phosphate ions hydroxyapatite crystallites. However, molecular basis EMP assembly remains poorly understood. This study shows self-assembly key EMPs, ameloblastin amelogenin, involves short linear amino acid motif is evolutionarily conserved from first tetrapods to man. Functionality this shown be essential for organization proper crystallites compact bundles determine structure mechanical resistance enamel.