| Summary: | 碩士 === 國立陽明大學 === 生化暨分子生物研究所 === 104 === Galectin-3 is the protein consisted of 112 disordered amino acids sequence of N-termini and 138 structural amino acids sequence of C-terminal carbohydrate recognition domain (CRD). Galectin-3 is widespread on mammalians body; including nuclear, plasma and circulatory system. Galectin-3 also has the wide biofunctions. We know that galectin-3 may involve the cell transformation, regulation of cell apoptosis and regulation of cell cycle. Some papers reported that disordered N-termini of galectin-3 may affect biofunctions of galectin-3. The papers showed that mutations on galectin-3 disordered N-termini avoid binding of galectin-3 and K-Ras protein, it will lead the cell continuously transform. And deletions on disordered N-termini of galectin-3 make the galectin-3 loss ability of transportation from nuclear to plasma. On the other research said that the lactose binging affinity of galectin-3 decreased as mutations on N-termini of galectin-3. It shows that N-termini of galectin-3 affects the protein functions by some interactions, but there are little research about N- and C- interaction. We want to know how the interaction between N- and C-terminus. We make three cysteines to alanines mutantion on disordered N-terminal of galectin-3, galetin-3-A10C, -A75C and -A100C. We made the NMR paramagnetic relaxation enhancement on three mutants. On this research, we found that disordered N-terminal of galectin-3 may interact with CRD and disordered N-terminal of galectin-3 may have the special attention of folding.
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