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

14 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

Keywords

Apoptosis
Galectin
Glycan
Proliferation
Signaling

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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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title = "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",

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.",

keywords = "Apoptosis, Galectin, Glycan, Proliferation, Signaling",

author = "Hans Ippel and Miller, {Michelle C.} and Berb{\'i}s, {Manuel A lvaro} and Dennis Suylen and Sabine Andr{\'e} and Hackeng, {Tilman M.} and Ca{\~n}ada, {F. Javier} and Christian Weber and Gabius, {Hans Joachim} and Jes{\'u}s Jim{\'e}nez-Barbero and Mayo, {Kevin H.}",

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AU - Ippel, Hans

AU - Miller, Michelle C.

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.

PY - 2015/4

Y1 - 2015/4

N2 - 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.

AB - 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.

KW - Apoptosis

KW - Galectin

KW - Glycan

KW - Proliferation

KW - Signaling

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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

Abstract

Keywords

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