1DY2

Murine collagen alpha1(XV), endostatin domain

Summary for 1DY2

• Entry DOI: 10.2210/pdb1dy2/pdb
• Related: 1DY0 1DY1 1DY2 1KOE
• Descriptor: COLLAGEN ALPHA1(XV) CHAIN, SULFATE ION (3 entities in total)
• Functional Keywords: angiogenesis inhibitor
• Biological source: MUS MUSCULUS (MOUSE)
• Total number of polymer chains: 1
• Total formula weight: 20181.94

Authors

Tisi, D.,Hohenester, E.,Sasaki, T.,Timpl, R. (deposition date: 2000-01-21, release date: 2001-01-21, Last modification date: 2023-12-06)

Primary citation

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

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: 10966814
DOI: 10.1006/JMBI.2000.3996

Experimental method

X-RAY DIFFRACTION (2 Å)