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. 2016 Mar 31;6:79. doi: 10.3389/fonc.2016.00079

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Copyright © 2016 Sindrewicz, Lian and Yu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Structural feature of galectin-3–TF interaction. Left panel: overall structure of galectin-3 CRD in complex with TF disaccharide (PDB 3AYA) (63). TF disaccharide (in stick model) binds to the CRD concave surf forms a E¹⁶⁵-water-R¹⁸⁶-water motif for TF recognition. Residues from strands S4–S6 (colored cyan) interact with the TF; L4 is the loop between S4 and S5. Middle panel: surface representation of strands S4–S6. Left panel: comparison between the structures of galectin-3 complex with the TF disaccharide and galectin-1 complex with Galβ1–3/4GlcNAc disaccharide (PDB 4XB1) (76). Galectin-3/TF is in green; galectin-1/Galβ1–3/4GlcNAc in white cartoon/yellow sticks. g1-L4 and g3-L4 are, respectively, the L4 loop for galectin-1 and galectin-3, which are found to adopt different conformations due to differences in the lengths and amino acid sequences of the two loops. D54 and R73 make up D⁵⁴-water-R⁷³-water motif that mediates ligand interactions.