Carboxyl-region of tuftelin mediates self-assembly.
Enamel biomineralization relies on a complex series of protein-protein interactions resulting in the formation of an enamel matrix. This protein matrix is subsequently replaced by a fully mineralized crystallite material. The enamel extracellular matrix is comprised principally by two gene products; the amelogenins and enamelins. The enamelins, including the 389 amino-acid, 44 kDa tuftelin, are a group of acidic proteins found in the enamel extracellular matrix. This study has employed the yeast two-hybrid system to investigate the ability of tuftelin to self-assemble and to define protein regions participating in tuftelin self-assembly. We show that for tuftelin the amino-acid residues 252 through 345 contain structurally relevant determinants for self-assembly.
Paine
M L
ML
University of Southern California, School of Dentistry, Los Angeles 90033, USA.
Deutsch
D
D
Snead
M L
ML
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002264:Carboxylic Acids; D002417:Cattle; D003746:Dental Enamel Proteins / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D001616:beta-Galactosidase / Q000378:metabolism
D002264:Carboxylic Acids; D003746:Dental Enamel Proteins; C038456:tuftelin; D001616:beta-Galactosidase