Complete primary structure of the collagen-binding domain of bovine fibronectin.
The complete amino acid sequence of the collagen-binding domain of bovine plasma fibronectin has been determined. The fragment, generated by digestion of fibronectin with plasmin and chymotrypsin, contains 340 residues (260-599 of fibronectin) with threonine and tryptophan as the amino-terminal and carboxyl-terminal amino acids, respectively. 24 half-cystines and no cysteines are present in the sequence. Three glucosamine-based oligosaccharide groups are attached to Asn-399, Asn-497 and to Asn-511, respectively. Two of the three types (I and II) [Petersen et al. (1983) Proc. Natl Acad. Sci. USA 80, 137-141] of internal homology occur in the fragment, namely four of the at least twelve stretches of type I sequence homology, 'fingers', and two stretches of type II homology. The type I homology is present in two other plasmic fragments from fibronectin, while the type II homology has been found in the collagen-binding domain only.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D001952:Bridged-Ring Compounds / Q000302:isolation & purification; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D003094:Collagen / Q000378:metabolism*; D004220:Disulfides / Q000302:isolation & purification; D005353:Fibronectins / Q000097:blood*; D006801:Humans; D010446:Peptide Fragments / Q000302:isolation & purification; D011485:Protein Binding; D013045:Species Specificity
D001952:Bridged-Ring Compounds; D004220:Disulfides; D005353:Fibronectins; D010446:Peptide Fragments; D003094:Collagen