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. Author manuscript; available in PMC: 2016 Sep 1.

Published in final edited form as: Prog Biophys Mol Biol. 2015 Apr 14;118(3):153–160. doi: 10.1016/j.pbiomolbio.2015.04.001

A. The netrin-1/DCC₄₅ structure. The interactions between the DCC FN4 domain and the netrin-1 laminin-like domain along with the relative clustering seen in the crystal packing are highlighted. Note that the FN5/EGF-3 binding site is shared with what is seen in Fig. 2 at site 1. B. Overlay of the crystal structures of the chicken netrin-1/mouse DCC₄₅ and the human netrin-1/human DCC₅₆ highlights complementarity. All three binding sites are designated as binding site 0, binding site 1, and binding site 2. Netrin-1 molecules are colored in green and light green, respectively, whereas DCC receptors are colored in red and magenta, respectively.

A. The netrin-1/DCC₄₅ structure. The interactions between the DCC FN4 domain and the netrin-1 laminin-like domain along with the relative clustering seen in the crystal packing are highlighted. Note that the FN5/EGF-3 binding site is shared with what is seen in Fig. 2 at site 1. B. Overlay of the crystal structures of the chicken netrin-1/mouse DCC₄₅ and the human netrin-1/human DCC₅₆ highlights complementarity. All three binding sites are designated as binding site 0, binding site 1, and binding site 2. Netrin-1 molecules are colored in green and light green, respectively, whereas DCC receptors are colored in red and magenta, respectively.