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

Hans Ippel, Michelle C. Miller, Manuel Alvaro Berbis, Dennis Suylen, Sabine Andre, Tilman M. Hackeng, F. Javier Canada, Christian Weber, Hans-Joachim Gabius, Jesus Jimenez-Barbero, Kevin H. Mayo*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

19 Citations (Web of Science)


Galectin-3, an adhesion/growth regulatory lectin, has a unique trimodular design consisting of the canonical carbohydrate recognition 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 total) will help understand the multi functionality of this potent cellular effector. Here, we report H-1, C-13, and N-15 chemical shift assignments as determined by heteronuclear NMR spectroscopy .
Original languageEnglish
Pages (from-to)59-63
JournalBiomolecular Nmr Assignments
Issue number1
Publication statusPublished - Apr 2015


  • Apoptosis
  • Galectin
  • Glycan
  • Proliferation
  • Signaling

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