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. 1999 Sep;10(9):2933–2943. doi: 10.1091/mbc.10.9.2933

Figure 1.

Figure 1

Models of one subunit of naturally occuring TN-C variants as isolated from chick embryo fibroblasts (CEF-TN) and of the deletion mutants used. The subunits consist of an N-terminal part involved in the oligomerization to hexamers (N-terminal domain and heptad repeats), followed by tenascin-type EGF-like repeats, FN type III repeats, and a domain homologous to the globular part of b- and g-fibrinogen. Alternatively spliced FN type III repeats are shown as gray rectangles. Each of the deletion mutants lacks one type of domains: TN-FB− lacks the fibrinogen globe, TN-FN− lacks all FN type III repeats, and TN-EGF− lacks all EGF-like repeats. All recombinant TN-C mutants were proven to occur as hexamers and to show expected dimensions and structural features (Fischer et al., 1997).