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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth. They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins [ ].Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units [ ]: the N-terminal region appears to contain β-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive β-turn segment and a "β-spiral"between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region [ ]. The β-spiral offers a probable site for interactions with Ca2+ ions.Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide [ ]. | Name | Amelogenin |
| Short Name | Amelogenin | Type | Family |
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