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The globular domains of type VI collagen are related to the collagen‐binding domains of cartilage matrix protein and von Willebrand factor.
Author(s) -
Koller E.,
Winterhalter K. H.,
Trueb B.
Publication year - 1989
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1989.tb03475.x
Subject(s) - cartilage oligomeric matrix protein , type (biology) , matrix (chemical analysis) , biology , microbiology and biotechnology , stereochemistry , chemistry , medicine , pathology , ecology , alternative medicine , chromatography , osteoarthritis
Type VI collagen is a transformation‐sensitive glycoprotein of the extracellular matrix of fibroblasts. We have isolated and sequenced several overlapping cDNA clones (4153 bp) which encode the entire alpha 2 subunit of chicken type VI collagen. The deduced amino acid sequence predicts that the alpha 2(VI) polypeptide consists of 1015 amino acid residues that are arranged in four domains: a hydrophobic signal peptide of 20 residues, an amino‐terminal globular domain of 228 residues, a collagenous segment of 335 residues and a carboxy‐terminal globular domain of 432 residues. The collagenous domain contains seven Arg‐Gly‐Asp tripeptide units, some of which are likely to be used as cell‐binding sites. The globular domains contain three homologous repeats with an average length of 180 amino acid residues. These repeats show a striking similarity to the collagen‐binding motifs found in von Willebrand factor and cartilage matrix protein. We therefore speculate that the globular domains of the alpha 2(VI) polypeptide may interact with collagenous structures.