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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin.

Angiogenesis inhibitors have gained much public attention recently as anti-cancer agents and several are currently in clinical trials, including angiostatin (Phase I, Thomas Jefferson University Hospital, Philadelphia, PA). We report here the bowl-shaped structure of angiostatin kringles 1-3, the first multi-kringle structure to be determined. All three kringle lysine-binding sites contain a bound bicine molecule of crystallization while the former of kringle 2 and kringle 3 are cofacial. Moreover, the separation of the kringle 2 and kringle 3 lysiner binding sites is sufficient to accommodate the alpha-helix of the 30 residue peptide VEK-30 found in the kringle 2/VEK-30 complex. Together the three kringles produce a central cavity suggestive of a unique domain where they may function in concert.[1]

References

  1. The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin. Abad, M.C., Arni, R.K., Grella, D.K., Castellino, F.J., Tulinsky, A., Geiger, J.H. J. Mol. Biol. (2002) [Pubmed]
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