1H, 13C, and 15N 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 A lvaro Berbís, Dennis Suylen, Sabine André, Tilman M. Hackeng, F. Javier Cañada, Christian Weber, Hans Joachim Gabius, Jesús Jiménez-Barbero, Kevin H. Mayo

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

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 1H, 13C, and 15N chemical shift assignments as determined by heteronuclear NMR spectroscopy.

Original languageEnglish (US)
Pages (from-to)59-63
Number of pages5
JournalBiomolecular NMR Assignments
Volume9
Issue number1
DOIs
StatePublished - Apr 2015

Bibliographical note

Funding Information:
This work was 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 and HJG, and European Research Council funding (ERC AdG °249929) to C.W. M.A.B. was supported by a FPI Ph.D. fellowship from the Spanish Ministry of Economy and Competitiveness. NMR instrumentation was provided with funds from the National Science Foundation (BIR-961477), the University of Minnesota Medical School, and the Minnesota Medical Foundation.

Publisher Copyright:
© 2014, Springer Science+Business Media Dordrecht.

Keywords

  • Apoptosis
  • Galectin
  • Glycan
  • Proliferation
  • Signaling

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