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 language | English (US) |
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Pages (from-to) | 59-63 |
Number of pages | 5 |
Journal | Biomolecular NMR Assignments |
Volume | 9 |
Issue number | 1 |
DOIs | |
State | Published - 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