(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignments for the 36 proline-containing, full length 29 kDa human chimera-type galectin-3.

9 p.Galectin-3 has a unique trimodular design consisting of the canonical lectin domain, a collagen-like tandem-repeat section and an N-terminal peptide with two sites for Ser phosphorylation. Structural characterization of the full-length protein with its non-lectin part (115 of 250 residues) will help understand the multifunctionality of this potent cellular effector. Here, we report 1H, 13C, and 15N chemical shift assignments as determined by heteronuclear NMR spectroscopy.This work was generously supported by a research grant from the National Cancer Institute (CA-096090) to KHM; EC funding (GlycoHIT, contract no. 260600; GLYCOPHARM, contract no. 217297) to JJB & HJG, and European Research Council funding (ERC AdG °249929) to CW. NMR instrumentation was provided with funds from the National Science Foundation (BIR-961477), the University of Minnesota Medical School, and the Minnesota Medical Foundation.Peer reviewe