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Connect Tissue Res. 1996;35(1-4):157-61.

Carboxyl-region of tuftelin mediates self-assembly.

Author information

1
University of Southern California, School of Dentistry, Los Angeles 90033, USA.

Abstract

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.

PMID:
9084654
[Indexed for MEDLINE]

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