The Carboxyl-terminal Domain of Phosphophoryn Contains Unique Extended Triplet Amino Acid Repeat Sequences Forming Ordered Carboxyl-Phosphate Interaction Ridges That May Be Essential in the Biomineralization Process
Copyright policy )The Carboxyl-terminal Domain of Phosphophoryn Contains Unique Extended Triplet Amino Acid Repeat Sequences Forming Ordered Carboxyl-Phosphate Interaction Ridges That May Be Essential in the Biomineralization Process
Phosphophoryns (PPs), a family of Asp and Ser(P)-rich dentin proteins, are considered to be archetypal regulators of several aspects of extracellular matrix (ECM) biomineralization. We have cloned a rat incisor PP gene, Dmp2, from our odontoblast cDNA library and localized it to mouse chromosome 5q21 within 2 centimorgans of Dmp1, another tooth-specific ECM protein. The carboxyl-terminal region of Dmp2 protein (60 residue % Ser, 31 residue % Asp) is divided into two domains, one with unique repetitive blocks of [DSS]n,3
- National Institute of Health Pakistan
- Northwestern University United States
- Northwestern University Philippines
- National Institutes of Health United States
Extracellular Matrix Proteins, Odontoblasts, Protein Conformation, Molecular Sequence Data, Chromosome Mapping, Gene Expression, Phosphoproteins, Rats, Mice, Calcification, Physiologic, Dentinogenesis Imperfecta, Dentin, Animals, Tissue Distribution, Amino Acid Sequence, RNA, Messenger, Repetitive Sequences, Nucleic Acid
Extracellular Matrix Proteins, Odontoblasts, Protein Conformation, Molecular Sequence Data, Chromosome Mapping, Gene Expression, Phosphoproteins, Rats, Mice, Calcification, Physiologic, Dentinogenesis Imperfecta, Dentin, Animals, Tissue Distribution, Amino Acid Sequence, RNA, Messenger, Repetitive Sequences, Nucleic Acid
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