Zinc-dependent dimers observed in crystals of human endostatin

AUTOR(ES)

Ding, Yuan-Hua

FONTE

The National Academy of Sciences

RESUMO

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.

Documentos Relacionados

• Characterization of a zinc-dependent transcriptional activator from Arabidopsis.
• Regulation of apoptotic potassium currents by coordinated zinc-dependent signalling
• A zinc-dependent epitope on the molecule of thymulin, a thymic hormone.
• Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis
• Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor