title: What the structure of angiostatin may tell us about its mechanism of action.
abstract: 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.
authors.affiliation: Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA. geiger@cem.msu.edu
authors.forename: J H
authors.initials: JH
authors.lastname: Geiger
authors.forename: S E
authors.initials: SE
authors.lastname: Cnudde
mesh_terms: 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
chemical_list: D020533:Angiogenesis Inhibitors; D043168:Angiostatins