(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.

Citation data:

Biomolecular NMR assignments, ISSN: 1874-270X, Vol: 9, Issue: 1, Page: 59-63

Publication Year:
2015
Usage 5
Link-outs 4
Abstract Views 1
Captures 7
Readers 7
Citations 6
Citation Indexes 6
PMID:
24504927
DOI:
10.1007/s12104-014-9545-3
Author(s):
Ippel, Hans, Miller, Michelle C, Berbís, Manuel Alvaro, Suylen, Dennis, André, Sabine, Hackeng, Tilman M, Cañada, F Javier, Weber, Christian, Gabius, Hans-Joachim, Jiménez-Barbero, Jesús, Mayo, Kevin H Show More Hide
Publisher(s):
Springer Nature
Tags:
Biochemistry, Genetics and Molecular Biology, Medicine
article description
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 .

This article has 0 Wikipedia mention.