Fig. 1

A. Schematic depiction of tenascin domain architecture from Homo sapiens. The four tenascin paralogs, tenascin-C (TNC), tenascin-R (TNR), tenascin-W (TNW) and tenascin-XB (TNXB), each has a signal peptide (sp) and heptad repeats that form a coiled-coil (c-c), followed by tenascin-type epidermal growth factor (EGF)-like domains, fibronectin type 3 (FN3) domains, and a C-terminal fibrinogen-related domain. Potential integrin-binding tripeptide amino acid motifs in the FN3 domains are indicated. B. The domain organization of the four tenascin paralogs found in the chicken Gallus gallus. P-rich = proline-rich. C. Schematic representation of the N-terminal region of H. sapiens TNC, showing signal peptide (sp), tenascin assembly domain with location of cysteine residues implicated in forming or stabilizing multimers and heptad repeats, and first EGF-like domain. D. The third FN3 domain of H. sapiens TNC is formed by seven β strands lettered A through G. (adapted from [116]). The integrin-binding motif arginine-glycine-aspartic acid (RGD) is present in an exposed loop between β strands F and G, and the integrin-binding motif isoleucine-aspartic acid-glycine (IDG) is present in an exposed loop between β strands B and C. The integrin receptors that recognize these motifs are indicated