title: (1)H, (13)C, and (15)N 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 (1)H, (13)C, and (15)N chemical shift assignments as determined by heteronuclear NMR spectroscopy .
authors: Department of Biochemistry and CARIM, University of Maastricht, Maastricht, The Netherlands.
authors: Hans
authors: H
authors: Ippel
authors: Michelle C
authors: MC
authors: Miller
authors: Manuel Alvaro
authors: MA
authors: Berbís
authors: Dennis
authors: D
authors: Suylen
authors: Sabine
authors: S
authors: André
authors: Tilman M
authors: TM
authors: Hackeng
authors: F Javier
authors: FJ
authors: Cañada
authors: Christian
authors: C
authors: Weber
authors: Hans-Joachim
authors: HJ
authors: Gabius
authors: Jesús
authors: J
authors: Jiménez-Barbero
authors: Kevin H
authors: KH
authors: Mayo
mesh_terms: D037502:Galectin 3 / Q000737:chemistry*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D011392:Proline; D011993:Recombinant Fusion Proteins / Q000737:chemistry*
chemical_list: D037502:Galectin 3; D011993:Recombinant Fusion Proteins; D011392:Proline