1ki0
From Proteopedia
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'''The X-ray Structure of Human Angiostatin''' | '''The X-ray Structure of Human Angiostatin''' | ||
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[[Category: Grella, D K.]] | [[Category: Grella, D K.]] | ||
[[Category: Tulinsky, A.]] | [[Category: Tulinsky, A.]] | ||
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Revision as of 19:46, 2 May 2008
The X-ray Structure of Human Angiostatin
Overview
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.
About this Structure
1KI0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin., Abad MC, Arni RK, Grella DK, Castellino FJ, Tulinsky A, Geiger JH, J Mol Biol. 2002 May 10;318(4):1009-17. PMID:12054798 Page seeded by OCA on Fri May 2 22:46:21 2008