Human chimera-type galectin-3: defining the critical tail length for high-affinity glycoprotein/cell surface binding and functional competition with galectin-1 in neuroblastoma cell growth regulation
Many human proteins have a modular design with receptor and structural domains. Using adhesion/growth-regulatory galectin-3 as model, we describe an interdisciplinary strategy to define the functional significance of its tail established by nine non-triple helical collagen-like repeats (I-IX) and th...
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| Main Authors: | , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
6 June 2014
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| In: |
Biochimie
Year: 2014, Volume: 104, Pages: 90-99 |
| DOI: | 10.1016/j.biochi.2014.05.010 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.biochi.2014.05.010 Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S0300908414001412 
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| Author Notes: | Jürgen Kopitz, Sabine Vértesy, Sabine André, Sabine Fiedler, Martina Schnölzer, Hans-Joachim Gabius |
| Summary: | Many human proteins have a modular design with receptor and structural domains. Using adhesion/growth-regulatory galectin-3 as model, we describe an interdisciplinary strategy to define the functional significance of its tail established by nine non-triple helical collagen-like repeats (I-IX) and the N-terminal peptide. Genetic engineering with sophisticated mass spectrometric product analysis provided the tools for biotesting, i.e. eight protein variants with different degrees of tail truncation. Evidently,various aspects of galectin-3 activity (cis binding and cell bridging) are affected by tail shortening in a different manner. Thus, this combined approach reveals an unsuspected complexity of structure-function relationship, encouraging further application beyond this chimera-type galectin. |
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| Item Description: | Gesehen am 16.09.2020 |
| Physical Description: | Online Resource |
| DOI: | 10.1016/j.biochi.2014.05.010 |