| Literature DB >> 9724722 |
Y H Ding1, K Javaherian, K M Lo, R Chopra, T Boehm, J Lanciotti, B A Harris, Y Li, R Shapiro, E Hohenester, R Timpl, J Folkman, D C Wiley.
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.Entities:
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Year: 1998 PMID： 9724722 PMCID： PMC27913 DOI： 10.1073/pnas.95.18.10443
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205