1ki0
From Proteopedia
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The X-ray Structure of Human Angiostatin
Contents |
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.
Disease
Known diseases associated with this structure: Conjunctivitis, ligneous OMIM:[173350], Plasminogen Tochigi disease OMIM:[173350], Plasminogen deficiency, types I and II OMIM:[173350], Thrombophilia, dysplasminogenemic OMIM:[173350]
About this Structure
1KI0 is a Single protein structure of sequence from Homo sapiens with BCN as ligand. Active as Plasmin, with EC number 3.4.21.7 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 Mon Nov 12 17:51:10 2007
