1bnl | pdb_00001bnl
ZINC DEPENDENT DIMERS OBSERVED IN CRYSTALS OF HUMAN ENDOSTATIN
Overview
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.
About this Structure
1BNL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Zinc-dependent dimers observed in crystals of human endostatin., Ding YH, Javaherian K, Lo KM, Chopra R, Boehm T, Lanciotti J, Harris BA, Li Y, Shapiro R, Hohenester E, Timpl R, Folkman J, Wiley DC, Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10443-8. PMID:9724722 Page seeded by OCA on Fri May 2 11:44:14 2008
