1BNL

ZINC DEPENDENT DIMERS OBSERVED IN CRYSTALS OF HUMAN ENDOSTATIN

Summary for 1BNL

• Entry DOI: 10.2210/pdb1bnl/pdb
• Descriptor: COLLAGEN XVIII, ZINC ION (2 entities in total)
• Functional Keywords: endostatin, collagen xviii, collagen, antiangiogenic, angiogenic, angiogenisis, cancer, zinc, extracellular matrix
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix (By similarity): P39060
• Total number of polymer chains: 4
• Total formula weight: 78610.32

Authors

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. (deposition date: 1998-07-30, release date: 1998-10-14, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.9 Å)