1KOE
ENDOSTATIN
Summary for 1KOE
Entry DOI | 10.2210/pdb1koe/pdb |
Descriptor | ENDOSTATIN (2 entities in total) |
Functional Keywords | angiogenesis inhibitor, collagen xviii, non-collageneous domain, heparin-binding domain |
Biological source | Mus musculus (house mouse) |
Cellular location | Secreted, extracellular space, extracellular matrix (By similarity): P39061 |
Total number of polymer chains | 1 |
Total formula weight | 18950.35 |
Authors | Hohenester, E.,Sasaki, T.,Olsen, B.R.,Timpl, R. (deposition date: 1998-01-22, release date: 1999-02-16, Last modification date: 2024-10-23) |
Primary citation | Hohenester, E.,Sasaki, T.,Olsen, B.R.,Timpl, R. Crystal structure of the angiogenesis inhibitor endostatin at 1.5 A resolution. EMBO J., 17:1656-1664, 1998 Cited by PubMed Abstract: A number of extracellular proteins contain cryptic inhibitors of angiogenesis. Endostatin is a 20 kDa C-terminal proteolytic fragment of collagen XVIII that potently inhibits endothelial cell proliferation and angiogenesis. Therapy of experimental cancer with endostatin leads to tumour dormancy and does not induce resistance. We have expressed recombinant mouse endostatin and determined its crystal structure at 1.5 A resolution. The structure reveals a compact fold distantly related to the C-type lectin carbohydrate recognition domain and the hyaluronan-binding Link module. The high affinity of endostatin for heparin is explained by the presence of an extensive basic patch formed by 11 arginine residues. Endostatin may inhibit angiogenesis by binding to the heparan sulphate proteoglycans involved in growth factor signalling. PubMed: 9501087DOI: 10.1093/emboj/17.6.1656 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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