H-1, C-13, and N-15 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 Alvaro Berbis; Dennis Suylen; Sabine Andre; Tilman M. Hackeng; F. Javier Canada; Christian Weber; Hans-Joachim Gabius; Jesus Jimenez-Barbero; Kevin H. Mayo

doi:10.1007/s12104-014-9545-3

H-1, C-13, and N-15 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 Alvaro Berbis, Dennis Suylen, Sabine Andre, Tilman M. Hackeng, F. Javier Canada, Christian Weber, Hans-Joachim Gabius, Jesus Jimenez-Barbero, Kevin H. Mayo^*

^*Corresponding author for this work

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

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

Original language	English
Pages (from-to)	59-63
Journal	Biomolecular Nmr Assignments
Volume	9
Issue number	1
DOIs	https://doi.org/10.1007/s12104-014-9545-3
Publication status	Published - Apr 2015

Keywords

Apoptosis
Galectin
Glycan
Proliferation
Signaling

Access to Document

10.1007/s12104-014-9545-3

Cite this

Ippel, H., Miller, M. C., Berbis, M. A., Suylen, D., Andre, S., Hackeng, T. M., Canada, F. J., Weber, C., Gabius, H.-J., Jimenez-Barbero, J., & Mayo, K. H. (2015). H-1, C-13, and N-15 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

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

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

author = "Hans Ippel and Miller, {Michelle C.} and Berbis, {Manuel Alvaro} and Dennis Suylen and Sabine Andre and Hackeng, {Tilman M.} and Canada, {F. Javier} and Christian Weber and Hans-Joachim Gabius and Jesus Jimenez-Barbero and Mayo, {Kevin H.}",

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Ippel, H, Miller, MC, Berbis, MA, Suylen, D, Andre, S, Hackeng, TM, Canada, FJ, Weber, C, Gabius, H-J, Jimenez-Barbero, J & Mayo, KH 2015, 'H-1, C-13, and N-15 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

TY - JOUR

T1 - H-1, C-13, and N-15 backbone and side-chain chemical shift assignments for the 36 proline-containing, full length 29 kDa human chimera-type galectin-3

AU - Ippel, Hans

AU - Miller, Michelle C.

AU - Berbis, Manuel Alvaro

AU - Suylen, Dennis

AU - Andre, Sabine

AU - Hackeng, Tilman M.

AU - Canada, F. Javier

AU - Weber, Christian

AU - Gabius, Hans-Joachim

AU - Jimenez-Barbero, Jesus

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

KW - Apoptosis

KW - Galectin

KW - Glycan

KW - Proliferation

KW - Signaling

U2 - 10.1007/s12104-014-9545-3

DO - 10.1007/s12104-014-9545-3

M3 - Article

C2 - 24504927

SN - 1874-2718

VL - 9

SP - 59

EP - 63

JO - Biomolecular Nmr Assignments

JF - Biomolecular Nmr Assignments

IS - 1

ER -