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What the structure of angiostatin may tell us about its mechanism of action Geiger JH; Cnudde SEJ Thromb Haemost 2004[Jan]; 2 (1): 23-34Originally discovered in 1994 by Folkman and coworkers, angiostatin was identified through its antitumor effects in mice and later shown to be a potent inhibitor of angiogenesis. An internal fragment of plasminogen, angiostatin consists of kringle domains that are known to be lysine-binding. The crystal structure of angiostatin was the first multikringle domain-containing structure to be published. This review will focus on what is known about the structure of angiostatin and its implications in function from the current literature.|Angiogenesis Inhibitors/chemistry/physiology[MESH]|Angiostatins/*chemistry/*physiology[MESH]|Animals[MESH]|Binding Sites[MESH]|Humans[MESH]|Kringles[MESH]|Models, Molecular[MESH]|Protein Binding[MESH]|Protein Conformation[MESH] |
