What the structure of angiostatin may tell us about its mechanism of action

J Thromb Haemost. 2004 Jan;2(1):23-34. doi: 10.1111/j.1538-7836.2004.00544.x.

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.

Publication types

  • Review

MeSH terms

  • Angiogenesis Inhibitors / chemistry
  • Angiogenesis Inhibitors / physiology
  • Angiostatins / chemistry*
  • Angiostatins / physiology*
  • Animals
  • Binding Sites
  • Humans
  • Kringles
  • Models, Molecular
  • Protein Binding
  • Protein Conformation

Substances

  • Angiogenesis Inhibitors
  • Angiostatins