| Autor: |
Ippel H; Department of Biochemistry and CARIM, University of Maastricht, Maastricht, The Netherlands., Miller MC, Berbís MA, Suylen D, André S, Hackeng TM, Cañada FJ, Weber C, Gabius HJ, Jiménez-Barbero J, Mayo KH |
| Jazyk: |
angličtina |
| Zdroj: |
Biomolecular NMR assignments [Biomol NMR Assign] 2015 Apr; Vol. 9 (1), pp. 59-63. Date of Electronic Publication: 2014 Feb 07. |
| DOI: |
10.1007/s12104-014-9545-3 |
| Abstrakt: |
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 . |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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