1DY0
Murine endostatin, crystal form II
Summary for 1DY0
| Entry DOI | 10.2210/pdb1dy0/pdb |
| Related | 1DY1 1DY2 1KOE |
| Descriptor | COLLAGEN ALPHA1(XVIII) CHAIN, ZINC ION (3 entities in total) |
| Functional Keywords | angiogenesis inhibitor |
| Biological source | MUS MUSCULUS (MOUSE) |
| Total number of polymer chains | 1 |
| Total formula weight | 20884.20 |
| Authors | Hohenester, E.,Sasaki, T.,Timpl, R. (deposition date: 2000-01-21, release date: 2000-04-11, Last modification date: 2024-11-06) |
| Primary citation | Hohenester, E.,Sasaki, T.,Mann, K.,Timpl, R. Variable Zinc Coordination in Endostatin J.Mol.Biol., 297:1-, 2000 Cited by PubMed Abstract: 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. PubMed: 10704302DOI: 10.1006/JMBI.2000.3553 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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