1dy0
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 7: | Line 16: | ||
==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]] | ||
| Line 19: | Line 28: | ||
[[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
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| 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
Page seeded by OCA on Thu Mar 20 10:46:20 2008
