1BNL

ZINC DEPENDENT DIMERS OBSERVED IN CRYSTALS OF HUMAN ENDOSTATIN

1BNL の概要

• エントリーDOI: 10.2210/pdb1bnl/pdb
• 分子名称: COLLAGEN XVIII, ZINC ION (2 entities in total)
• 機能のキーワード: endostatin, collagen xviii, collagen, antiangiogenic, angiogenic, angiogenisis, cancer, zinc, extracellular matrix
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix (By similarity): P39060
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 78610.32

構造登録者

Ding, Y.-H.,Javaherian, K.,Lo, K.-M.,Chopra, R.,Boehm, T.,Lanciotti, J.,Harris, B.A.,Li, Y.,Shapiro, R.,Hohenester, E.,Timpl, R.,Folkman, J.,Wiley, D.C. (登録日: 1998-07-30, 公開日: 1998-10-14, 最終更新日: 2024-10-16)

主引用文献

Ding, Y.H.,Javaherian, K.,Lo, K.M.,Chopra, R.,Boehm, T.,Lanciotti, J.,Harris, B.A.,Li, Y.,Shapiro, R.,Hohenester, E.,Timpl, R.,Folkman, J.,Wiley, D.C.
Zinc-dependent dimers observed in crystals of human endostatin.
Proc.Natl.Acad.Sci.USA, 95:10443-10448, 1998

PubMed Abstract: The crystal structure of human endostatin reveals a zinc-binding site. Atomic absorption spectroscopy indicates that zinc is a constituent of both human and murine endostatin in solution. The human endostatin zinc site is formed by three histidines at the N terminus, residues 1, 3, and, 11, and an aspartic acid at residue 76. The N-terminal loop ordered around the zinc makes a dimeric contact in human endostatin crystals. The location of the zinc site at the amino terminus, immediately adjacent to the precursor cleavage site, suggests the possibility that the zinc may be involved in activation of the antiangiogenic activity following cleavage from the inactive collagen XVIII precursor or in the cleavage process itself.

PubMed: 9724722
DOI: 10.1073/pnas.95.18.10443

実験手法

X-RAY DIFFRACTION (2.9 Å)