1DY0

Murine endostatin, crystal form II

1DY0 の概要

• エントリーDOI: 10.2210/pdb1dy0/pdb
• 関連するPDBエントリー: 1DY1 1DY2 1KOE
• 分子名称: COLLAGEN ALPHA1(XVIII) CHAIN, ZINC ION (3 entities in total)
• 機能のキーワード: angiogenesis inhibitor
• 由来する生物種: MUS MUSCULUS (MOUSE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20884.20

構造登録者

Hohenester, E.,Sasaki, T.,Timpl, R. (登録日: 2000-01-21, 公開日: 2000-04-11, 最終更新日: 2024-11-06)

主引用文献

Hohenester, E.,Sasaki, T.,Mann, K.,Timpl, R.
Variable Zinc Coordination in Endostatin
J.Mol.Biol., 297:1-, 2000

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: 10704302
DOI: 10.1006/JMBI.2000.3553

実験手法

X-RAY DIFFRACTION (2.2 Å)