1dy0
From Proteopedia
(New page: 200px<br /><applet load="1dy0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dy0, resolution 2.20Å" /> '''MURINE ENDOSTATIN, C...) |
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| - | [[Image:1dy0.gif|left|200px]]<br /><applet load="1dy0" size=" | + | [[Image:1dy0.gif|left|200px]]<br /><applet load="1dy0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dy0, resolution 2.20Å" /> | caption="1dy0, resolution 2.20Å" /> | ||
'''MURINE ENDOSTATIN, CRYSTAL FORM II'''<br /> | '''MURINE ENDOSTATIN, CRYSTAL FORM II'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Endostatin is a proteolytic fragment of collagen XVIII that potently | + | Endostatin is a proteolytic fragment of collagen XVIII that potently inhibits angiogenesis and tumour growth. Human endostatin contains a zinc ion, bound near the N terminus, which was not observed in the original structure of mouse endostatin at pH 5. Controversial data exist on the role of this zinc ion in the anti-tumour activity. We report two new crystal structures of mouse endostatin at pH 8.5 with bound zinc. One crystal form shows a metal ion coordination similar to that in human endostatin (His132, His134, His142, Asp207), but the conformation of the N-terminal segment is different. In the other crystal form, Asp136 replaces His132 as a zinc ligand. Site-directed mutagenesis of zinc-binding residues demonstrates that both coordination geometries occur in solution. The large degree of structural heterogeneity of the zinc-binding site has implications for endostatin function. We conclude that zinc is likely to play a structural rather than a critical functional role in endostatin. |
==About this Structure== | ==About this Structure== | ||
| - | 1DY0 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 ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1DY0 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=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DY0 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 12:21:43 2008'' |
Revision as of 10:21, 21 February 2008
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MURINE ENDOSTATIN, CRYSTAL FORM II
Overview
Endostatin is a proteolytic fragment of collagen XVIII that potently inhibits angiogenesis and tumour growth. Human endostatin contains a zinc ion, bound near the N terminus, which was not observed in the original structure of mouse endostatin at pH 5. Controversial data exist on the role of this zinc ion in the anti-tumour activity. We report two new crystal structures of mouse endostatin at pH 8.5 with bound zinc. One crystal form shows a metal ion coordination similar to that in human endostatin (His132, His134, His142, Asp207), but the conformation of the N-terminal segment is different. In the other crystal form, Asp136 replaces His132 as a zinc ligand. Site-directed mutagenesis of zinc-binding residues demonstrates that both coordination geometries occur in solution. The large degree of structural heterogeneity of the zinc-binding site has implications for endostatin function. We conclude that zinc is likely to play a structural rather than a critical functional role in endostatin.
About this Structure
1DY0 is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Variable zinc coordination in endostatin., Hohenester E, Sasaki T, Mann K, Timpl R, J Mol Biol. 2000 Mar 17;297(1):1-6. PMID:10704302
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