1dy0
From Proteopedia
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|PDB= 1dy0 |SIZE=350|CAPTION= <scene name='initialview01'>1dy0</scene>, resolution 2.20Å | |PDB= 1dy0 |SIZE=350|CAPTION= <scene name='initialview01'>1dy0</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dy0 OCA], [http://www.ebi.ac.uk/pdbsum/1dy0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dy0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Sasaki, T.]] | [[Category: Sasaki, T.]] | ||
[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
| - | [[Category: ZN]] | ||
[[Category: angiogenesis inhibitor]] | [[Category: angiogenesis inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:51:07 2008'' |
Revision as of 16:51, 30 March 2008
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| , resolution 2.20Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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