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

Anne George, Leslie Bannon, Boris Sabsay, Jerry W. Dillon, James Malone, Arthur Veis*, Nancy A. Jenkins, Debra J. Gilbert, Neal G. Copeland

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

172 Scopus citations

Abstract

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 Dmp 1, 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≤14, the other with [SD]m = 2,3. Conformational analysis shows the phosphorylated form of the [DS*S*]n repeats to have a unique structure with well defined ridges of phosphates and carboxyls available for counter ion binding. The [S*D]m domains have different phosphate and carboxylate interaction edges and thus different calcium ion and apatite surface binding properties. These two domains and the colocalization of Dmp1 and Dmp2 genes at a position equivalent to the dentinogenesis imperfecta type II location on human 4q21 all suggest that the PPs are indeed involved in some aspect of ECM mineralization.

Original languageEnglish (US)
Pages (from-to)32869-32873
Number of pages5
JournalJournal of Biological Chemistry
Volume271
Issue number51
DOIs
StatePublished - 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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