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  • Title: Discovery of a new sialic acid binding region that regulates Siglec-7.
    Author: Yamakawa N, Yasuda Y, Yoshimura A, Goshima A, Crocker PR, Vergoten G, Nishiura Y, Takahashi T, Hanashima S, Matsumoto K, Yamaguchi Y, Tanaka H, Kitajima K, Sato C.
    Journal: Sci Rep; 2020 May 26; 10(1):8647. PubMed ID: 32457377.
    Abstract:
    Siglec-7 is a human CD33-like siglec, and is localised predominantly on human natural killer (NK) cells and monocytes. Siglec-7 is considered to function as an immunoreceptor in a sialic acid-dependent manner. However, the underlying mechanisms linking sialic acid-binding and function remain unknown. Here, to gain new insights into the ligand-binding properties of Siglec-7, we carried out in silico analysis and site-directed mutagenesis, and found a new sialic acid-binding region (site 2 containing R67) in addition to the well-known primary ligand-binding region (site 1 containing R124). This was supported by equilibrium dialysis, STD-NMR experiments, and inhibition analysis of GD3-binding toward Siglec-7 using synthetic sialoglycoconjugates and a comprehensive set of ganglioside-based glycoconjugates. Our results suggest that the two ligand-binding sites are potentially controlled by each other due to the flexible conformation of the C-C' loop of Siglec-7.
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