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  • Title: [Site-directed mutagenesis of the gene of Echistatin Leu14-Lys15-Glu16].
    Author: Li H, Li X, Hu M.
    Journal: Yi Chuan Xue Bao; 1996; 23(2):163-8. PubMed ID: 8695184.
    Abstract:
    In order to probe relationship of inhibition activity of platelet aggregation and RGD conformation beneficial to binding in Echistatin, we used the site-directed mutation technique to install another RGD sequence into one of irregular loops retaining a degree of conformational flexibility and substituting Leu-14, Lys-15, Glu-16 of (Leu-28) Echistatin. The mutant (Arg-14, Gly-15, Asp-16, Leu-28) Echistatin did not lose its inhibition activity of platelet aggregation; however, it showed at least as high activity as (Leu-28) Echistatin, or even a little higher than (Leu-28) Echistatin. This suggested that both RGD sequences inserted in one loop with a degree of conformational flexibility. The original RGD (Arg-24, Gly-25, Asp-26) motif projecting significantly from the surface of the scaffold or core might contribute synergistically to the function of inhibiting platelet aggregation induced by 10 mumol/ L ADP (final concentration). These results are useful in the elucidation of the relationship of structure and function of Echistatin-like disintegrins and GPIIb/IIIa-like integrins.
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