Abstract
The non-classical secretion of Human Fibroblast Growth Factor-1 (hFGF-1) is a poorly understood process. hFGF-1 is known to interact with the Ca2+ binding C2B chaperone protein, which escorts FGF-1 to the cytoplasmic side of the cell membrane. The dual-alpha-helical structure of C2B has been well characterized. It not only contains Ca2+ binding sites, but is also binds to Cu2+. Recent studies suggest that Cu2+ shares common binding sites with Ca2+. In the presence of these two metal ions, the 2 binding sites for copper assists in the formation of the hFGF-1/C2B complex, specifically at the amino acid residues Cys-277, Phe-278, Ser-279, Leu-294, Asp-309, Gly-320, Lys-331, Lys-324 and Gly-384. In order to gain a better understanding of this complex reaction, it is desirable to observe the structural stability of the C2B domain of Synaptotagmin B by using multi-dimensional NMR spectroscopy and other biophysical methods. Non-classical release of hFGF-1 presents a promising target for treatment of cardiovascular, oncologic, and inflammatory disorders. Characterization of the three-dimensional solution structure of the complex will provide valuable insights on the design of novel therapeutic principle against hFGF-1-induced pathogenesis.
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