1dy2: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dy2.gif|left|200px]]<br /><applet load="1dy2" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dy2, resolution 2.00&Aring;" />
caption="1dy2, resolution 2.00&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DY2 OCA].  
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]]


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