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. Author manuscript; available in PMC: 2016 Dec 1.
Published in final edited form as: Biochim Biophys Acta. 2015 Sep 12;1850(12):2422–2438. doi: 10.1016/j.bbagen.2015.09.007

FIGURE 1.

FIGURE 1

Schematic model of the α1 chain of human collagen XVIII. The human collagen XV α1 chain is structurally homologous. They belong to a collagen subfamily, the multiplexins, on the basis of their central triple-helical domain (green boxes) interrupted by non-collagenous sequences. They contain an extended non-collagenous N-terminal domain, which, in collagen XVIII, can undergo alternative splicing (pale orange boxes), and a non-collagenous C-terminal domain (NC1; blue). The homotrimers (dark blue circles); a hinge domain (blue lines), which is highly susceptible to proteolytic processing; and a C-terminal endostatin domain (blue ovals), which has angiostatic properties. [Adapted from Iozzo [37] with permission from Nature Publishing Group.]