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

20 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

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

Keywords

Apoptosis
Galectin
Glycan
Proliferation
Signaling

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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

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

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AU - Suylen, Dennis

AU - André, Sabine

AU - Hackeng, Tilman M.

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