The primary structure of a cell-binding bone sialoprotein.
We have determined the amino acid sequence of rat bone sialoprotein ( BSP). The sequence deduced from a 1974-base pair cDNA encodes a protein of 320 residues, including a 16-residues long signal peptide. The mature BSP has a molecular mass of 33,600 and contains predominantly glutamic acid and glycine residues, which constitute 32% of all residues. The glutamic acid residues are typically distributed in clusters of up to 10 consecutive residues. The tissue distribution of BSP mRNA suggests that the protein may be a unique product of cells in bone tissue. BSP contains an Arg-Gly-Asp sequence, which presumably is responsible for its cell binding properties (Oldberg, A., Franzén, A., Heinegård, D., Pierschbacher, M., and Ruoslahti, E. (1988) J. Biol. Chem. 263, 19433-19436).[1]References
- The primary structure of a cell-binding bone sialoprotein. Oldberg, A., Franzén, A., Heinegård, D. J. Biol. Chem. (1988) [Pubmed]
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