1dy2
From Proteopedia
(New page: 200px<br /><applet load="1dy2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dy2, resolution 2.00Å" /> '''MURINE COLLAGEN ALPH...) |
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| - | [[Image:1dy2.gif|left|200px]]<br /><applet load="1dy2" size=" | + | [[Image:1dy2.gif|left|200px]]<br /><applet load="1dy2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dy2, resolution 2.00Å" /> | caption="1dy2, resolution 2.00Å" /> | ||
'''MURINE COLLAGEN ALPHA1(XV), ENDOSTATIN DOMAIN'''<br /> | '''MURINE COLLAGEN ALPHA1(XV), ENDOSTATIN DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Endostatin is a fragment of the C-terminal domain NC1 of collagen XVIII | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1DY2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1DY2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DY2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: angiogenesis inhibitor]] | [[Category: angiogenesis inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:44 2008'' |
Revision as of 10:21, 21 February 2008
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MURINE COLLAGEN ALPHA1(XV), ENDOSTATIN DOMAIN
Overview
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.
About this Structure
1DY2 is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity., Sasaki T, Larsson H, Tisi D, Claesson-Welsh L, Hohenester E, Timpl R, J Mol Biol. 2000 Sep 1;301(5):1179-90. PMID:10966814
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