1dy0: Difference between revisions
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[[Image:1dy0.gif|left|200px]] | [[Image:1dy0.gif|left|200px]] | ||
'''MURINE ENDOSTATIN, CRYSTAL FORM II''' | {{Structure | ||
|PDB= 1dy0 |SIZE=350|CAPTION= <scene name='initialview01'>1dy0</scene>, resolution 2.20Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''MURINE ENDOSTATIN, CRYSTAL FORM II''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DY0 is a [ | 1DY0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DY0 OCA]. | ||
==Reference== | ==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:[http:// | Variable zinc coordination in endostatin., Hohenester E, Sasaki T, Mann K, Timpl R, J Mol Biol. 2000 Mar 17;297(1):1-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10704302 10704302] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: angiogenesis inhibitor]] | [[Category: angiogenesis inhibitor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:46:20 2008'' | ||
Revision as of 08:46, 20 March 2008
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| 1dy0, resolution 2.20Å | |||||||||||||
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| Ligands: | ZN | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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