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

doi:10.1007/s12104-014-9545-3

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

Biochemistry, Molecular Biology, and Biophysics (TMED)

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	59-63
Number of pages	5
Journal	Biomolecular NMR Assignments
Volume	9
Issue number	1
DOIs	https://doi.org/10.1007/s12104-014-9545-3
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

Publisher link

10.1007/s12104-014-9545-3

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Ippel, H., Miller, M. C., Berbís, M. A. L., Suylen, D., André, S., Hackeng, T. M., Cañada, F. J., Weber, C., Gabius, H. J., Jiménez-Barbero, J., & Mayo, K. H. (2015). 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. Biomolecular NMR Assignments, 9(1), 59-63. https://doi.org/10.1007/s12104-014-9545-3

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. / Ippel, Hans; Miller, Michelle C.; Berbís, Manuel A lvaro; Suylen, Dennis; André, Sabine; Hackeng, Tilman M.; Cañada, F. Javier; Weber, Christian; Gabius, Hans Joachim; Jiménez-Barbero, Jesús; Mayo, Kevin H.

In: Biomolecular NMR Assignments, Vol. 9, No. 1, 04.2015, p. 59-63.

Research output: Contribution to journal › Article › peer-review

Ippel, H, Miller, MC, Berbís, MAL, Suylen, D, André, S, Hackeng, TM, Cañada, FJ, Weber, C, Gabius, HJ, Jiménez-Barbero, J & Mayo, KH 2015, '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', Biomolecular NMR Assignments, vol. 9, no. 1, pp. 59-63. https://doi.org/10.1007/s12104-014-9545-3

Ippel, Hans ; Miller, Michelle C. ; Berbís, Manuel A lvaro ; Suylen, Dennis ; André, Sabine ; Hackeng, Tilman M. ; Cañada, F. Javier ; Weber, Christian ; Gabius, Hans Joachim ; Jiménez-Barbero, Jesús ; Mayo, Kevin H. / 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. In: Biomolecular NMR Assignments. 2015 ; Vol. 9, No. 1. pp. 59-63.

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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.",

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AU - Berbís, Manuel A lvaro

AU - Suylen, Dennis

AU - André, Sabine

AU - Hackeng, Tilman M.

AU - Cañada, F. Javier

AU - Weber, Christian

AU - Gabius, Hans Joachim

AU - Jiménez-Barbero, Jesús

AU - Mayo, Kevin H.

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