What the structure of angiostatin may tell us about its mechanism of action.
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.
Geiger
J H
JH
Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA. geiger@cem.msu.edu
Cnudde
S E
SE
D020533:Angiogenesis Inhibitors / Q000737:chemistry / Q000502:physiology; D043168:Angiostatins / Q000737:chemistry* / Q000502:physiology*; D000818:Animals; D001665:Binding Sites; D006801:Humans; D018082:Kringles; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation
D020533:Angiogenesis Inhibitors; D043168:Angiostatins