| Primary Identifier | IPR004116 | Type | Family |
| Short Name | Amelogenin |
| description | Amelogenins, cell adhesion proteins, play a role in the biomineralisation ofteeth. They seem to regulate formation of crystallites during the secretorystage of tooth enamel development and are thought to play a major role inthe structural organisation and mineralisation of developing enamel. Theextracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins [].Circulardichroism studies of porcine amelogenin have shown that the proteinconsists of 3 discrete folding units []: the N-terminal region appears tocontain β-strand structures, while the C-terminal region displayscharacteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain arepetitive β-turn segment and a "β-spiral"between Gln112 and Leu138,which sequester a (Pro, Leu, Gln) rich region []. The β-spiraloffers a probable site for interactions with Ca2+ ions.Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplasticamelogenesis imperfecta, a disease characterised by defective enamel. A 9bpdeletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disruptingthe 16-residue (Met1-Ala16) amelogenin signal peptide []. |
