1KI0

The X-ray Structure of Human Angiostatin

Summary for 1KI0

• Entry DOI: 10.2210/pdb1ki0/pdb
• Descriptor: ANGIOSTATIN, BICINE (3 entities in total)
• Functional Keywords: kringle domains, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P00747
• Total number of polymer chains: 1
• Total formula weight: 29573.78

Authors

Abad, M.C.,Arni, R.K.,Grella, D.K.,Castellino, F.J.,Tulinsky, A.,Geiger, J.H. (deposition date: 2001-12-02, release date: 2002-05-29, Last modification date: 2024-11-06)

Primary citation

Abad, M.C.,Arni, R.K.,Grella, D.K.,Castellino, F.J.,Tulinsky, A.,Geiger, J.H.
The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin.
J.Mol.Biol., 318:1009-1017, 2002

PubMed Abstract: 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.

PubMed: 12054798
DOI: 10.1016/S0022-2836(02)00211-5

Experimental method

X-RAY DIFFRACTION (1.75 Å)