1DY2
Murine collagen alpha1(XV), endostatin domain
1DY2 の概要
| エントリーDOI | 10.2210/pdb1dy2/pdb |
| 関連するPDBエントリー | 1DY0 1DY1 1DY2 1KOE |
| 分子名称 | COLLAGEN ALPHA1(XV) CHAIN, SULFATE ION (3 entities in total) |
| 機能のキーワード | angiogenesis inhibitor |
| 由来する生物種 | MUS MUSCULUS (MOUSE) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 20181.94 |
| 構造登録者 | |
| 主引用文献 | Sasaki, T.,Larsson, H.,Tisi, D.,Claesson-Welsh, L.,Hohenester, E.,Timpl, R. Endostatin Derived from Collagens Xv and Xviii Differ in Structural and Binding Properties, Tissue Distribution and Anti-Angiogenic Activity J.Mol.Biol., 301:1179-, 2000 Cited by PubMed Abstract: Endostatin is a fragment of the C-terminal domain NC1 of collagen XVIII that inhibits angiogenesis and tumor growth. We report the characterization of a collagen XV endostatin analogue and its parent NC1 domain, obtained by recombinant expression in mammalian cells. Both NC1 domains contain a trimerization domain, a hinge region that is more sensitive to proteolysis in collagen XVIII and the endostatin domain. Unlike endostatin-XVIII, endostatin-XV does not bind zinc or heparin, which is explained by the crystal structure of endostatin-XV. The collagen XV and XVIII fragments inhibited chorioallantoic membrane angiogenesis induced by basic fibroblast growth factor (FGF-2) or vascular endothelial growth factor (VEGF), but there are striking differences depending on which cytokine is used and whether free endostatins or NC1 domains are applied. The collagen XV and XVIII fragments showed a similar binding repertoire for extracellular matrix proteins. Differences were found in the immunohistological localization in vessel walls and basement membrane zones. Together, these data indentify endostatin-XV as an angiogenesis inhibitor, which differs from endostatin-XVIII in several important functional details. PubMed: 10966814DOI: 10.1006/JMBI.2000.3996 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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