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. Author manuscript; available in PMC: 2012 Jan 1.
Published in final edited form as: Exp Eye Res. 2010 Nov 24;92(1):2–3. doi: 10.1016/j.exer.2010.11.009

Figure 1.

Figure 1

A. Genomic organization and protein structure of galectin-3. The Roman numerals indicate the position of the exons. The size of introns and polypeptide coding sequences are given in kb and bp, respectively. Galectin-3 consists of an N-terminal domain, 100-150 amino acids according to species of origin, and a C-terminal domain of about 135 amino acids, containing one carbohydrate recognition domain (CRD). B. Galectin-3 assembles in pentamer formation in the presence of multivalent ligands, in a process mediated through the N-terminal domain. At the cell surface, galectin-3 participates in cell-cell and cell-extracellular matrix (ECM) interactions, receptor clustering and signal transduction, and in the formation of glycoprotein-galectin lattices.