Open AccessComplete primary structure of the collagen‐binding domain of bovine fibronectin
Author(s) -
SKORSTENGAARD Karna,
THØGERSEN Hans Chr.,
PETERSEN Torben Ellebæk
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08092.x
Subject(s) - fibronectin , chemistry , computational biology , biology , biochemistry , extracellular matrix
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.