Comparative genomics and structure prediction of dental matrix proteins.

R. K. Krishnaraju, T. C. Hart, Titus Schleyer

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Non-collagenous matrix proteins secreted by the ameloblasts (amelogenin) and odontoblasts (osteocalcin) play important roles in the mineralization of enamel and dentin. In this study, comparative genomics approaches were used to identify the functional domains and model the three-dimensional structure of amelogenin and osteocalcin, respectively. Multiple sequence analysis of amelogenin in different species showed a high degree of sequence conservation at the nucleotide and protein levels. At the protein level, motifs (a sequence pattern that occurs repeatedly in a group of related proteins or genes), conserved domains, secondary structural characteristics, and functional sites of amelogenin from lower phyla were similar to those of the higher-level mammals, reflecting the high degree of sequence conservation during vertebrate evolution. Osteocalcin, produced by both odontoblasts and osetoblasts, also showed sequence similarity between species. Three-dimensional structure predictions developed by modeling of conserved domains of osteocalcin supported a role for glutamic acid residues in the calcium mineralization process.

Original languageEnglish
Pages (from-to)100-103
Number of pages4
JournalAdvances in dental research
Volume17
StatePublished - 2003
Externally publishedYes

Fingerprint

Amelogenin
Osteocalcin
Genomics
Tooth
Odontoblasts
Proteins
Ameloblasts
Dentin
Dental Enamel
Sequence Analysis
Vertebrates
Glutamic Acid
Mammals
Nucleotides
Calcium

Cite this

Comparative genomics and structure prediction of dental matrix proteins. / Krishnaraju, R. K.; Hart, T. C.; Schleyer, Titus.

In: Advances in dental research, Vol. 17, 2003, p. 100-103.

Research output: Contribution to journalArticle

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