Ca2+ Binding to α-Synuclein Regulates Ligand Binding and Oligomerization
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چکیده
منابع مشابه
The interplay between lipids and dopamine on α-synuclein oligomerization and membrane binding
The deposition of α-syn (α-synuclein) as amyloid fibrils and the selective loss of DA (dopamine) containing neurons in the substantia nigra are two key features of PD (Parkinson's disease). α-syn is a natively unfolded protein and adopts an α-helical conformation upon binding to lipid membrane. Oligomeric species of α-syn have been proposed to be the pathogenic species associated with PD becaus...
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پروتئینها فراوان تری مولکولهای آلی در بدن جانداران می باشند. آنزیم ها یکی از مهمترین نوع پروتئینهای کروی می باشند که بعضی از فعالیتهای حیات بدانها وابسته است . لیزوزیم اولین آنزیم شناخته شده است . این آنزیم دارای 129 واحد اسید آمینه در زنجیر پلی پپتیدی و چهار پیوند سیستئین درون زنجیری می باشد. لیزوزیم به دلیل دارا بودن اسید آمینه های باردار توان پذیرش بعضی از لیگاندها را دارا می باشد. در این پا...
15 صفحه اولCopper(II) Binding to α-Synuclein, the Parkinson’s Protein
Variations in tryptophan fluorescence intensities confirm that copper(II) interacts with alpha-synuclein, a protein implicated in Parkinson's disease. Trp4 fluorescence decay kinetics measured for the F4W protein show that Cu(II) binds tightly (Kd 100 nM) near the N-terminus at pH 7. Work on a F4W/H50S mutant indicates that a histidine imidazole is not a ligand in this high-affinity site.
متن کاملManganese and Iron Binding to Human Transferrin
The characteristics of manganese and iron binding to human apotransferrin (apo-tf) have been investigated and compared in this study. Both metal ions were taken up by human apo-tf and formed complexes, with the maximum absorbances observed at 410 and 340 nm for manganese-transferrin (Mn-tf) and 465 nm for iron-transferrin (Fe-tf). Addition of manganese (1.5 µg/ml) to the reaction mixture contai...
متن کاملDopamine-Mediated Oxidation of Methionine 127 in α-Synuclein Causes Cytotoxicity and Oligomerization of α-Synuclein
Parkinson's disease (PD) is a neurodegenerative disorder characterized by the selective loss of dopaminergic neurons and the presence of Lewy bodies. Many recent studies focused on the interaction between α-synuclein (α-syn) and dopamine in the pathogenesis of PD, and fluorescent anisotropy suggested that the C-terminal region of α-syn may be a target for modification by dopamine. However, it i...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m101181200