Secondary structure predictions for rat osteopontin.
Five computerized methods were used to predict the secondary structure of osteopontin - a bone-derived cell attachment protein. The amino terminal one-fifth and the carboxy terminal one-third of the 301 amino acid protein contain eight alpha helices (41% of the total residues). The middle of the molecule contains a very acidic region of no predicted structure followed by two segments of beta structure which flank the cell attachment site of osteopontin. Examination of the amino acid sequence also revealed a potential calcium binding loop and two potential heparin binding sites.
Prince
C W
CW
Department of Nutrition Sciences, University of Alabama, Birmingham 35294.
D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D008969:Molecular Sequence Data; D053495:Osteopontin; D010750:Phosphoproteins; D011487:Protein Conformation; D051381:Rats; D012795:Sialoglycoproteins
D010750:Phosphoproteins; D012795:Sialoglycoproteins; C506897:Spp1 protein, rat; D053495:Osteopontin