Ocellatusin is a new RGD-containing short monomeric disintegrin. It is a better inhibitor of α5β1 integrin and a more potent inducer of the expression of a ligand-induced binding site epitope on β1 integrin subunit than echistatin. In further contrast to echistatin, ocellatusin has a direct chemotactic stimulus on human neutrophils in vitro. The distinct effects of these two close evolutionarily related disintegrins might be explained by the presence of methionine-22 and histidine-29 in the RGD loop of ocellatusin, which are arginine and aspartic acid, respectively, in echistatin. These mutations may modulate the conformation and/or recognition properties of the integrin-binding loop of ocellatusin. © 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Smith, J. B., Theakston, R. D. G., Coelho, A. L. J., Barja-Fidalgo, C., Calvete, J. J., & Marcinkiewicz, C. (2002). Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus. FEBS Letters, 512(1–3), 111–115. https://doi.org/10.1016/S0014-5793(02)02233-0