What the structure of angiostatin may tell us about its mechanism of action |
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Authors: | J H Geiger S E Cnudde |
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Institution: | Department of Chemistry and;Department of Biochemistry, Michigan State University, East Lansing, MI, USA |
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Abstract: | Summary. Originally 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. |
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Keywords: | angiostatin kringle lysine-binding site (LBS) plasminogen |
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