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What the structure of angiostatin may tell us about its mechanism of action
Author(s) -
Geiger J. H.,
Cnudde S. E.
Publication year - 2004
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1111/j.1538-7836.2004.00544.x
Subject(s) - angiostatin , kringle domain , angiogenesis , mechanism of action , structure function , function (biology) , focus (optics) , lysine , mechanism (biology) , chemistry , microbiology and biotechnology , biology , biochemistry , cancer research , amino acid , physics , in vitro , recombinant dna , gene , optics , particle physics , quantum mechanics
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.