Zinc-dependent dimers observed in crystals of human endostatin

被引：121

作者：

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

机构：

[1] Childrens Hosp, Dept Surg, Boston, MA 02115 USA

[2] Harvard Univ, Sch Med, Dept Surg, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Dept Cellular Biol, Boston, MA 02115 USA

[4] Harvard Univ, Howard Hughes Med Inst, Dept Cellular & Mol Biol, Cambridge, MA 02138 USA

[5] Childrens Hosp, Howard Hughes Med Inst, Mol Med Lab, Dept Med, Boston, MA 02115 USA

[6] Lexigen Pharmaceut Corp, Lexington, MA 02173 USA

[7] Harvard Univ, Sch Med, Ctr Biochem & Biophys Sci & Med, Dept Pathol, Boston, MA 02115 USA

[8] Univ London Birkbeck Coll, Dept Crystallog, London WC1E 7HX, England

[9] Max Planck Inst Biochem, D-82152 Martinsried, Germany

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1998年 / 95卷 / 18期

关键词：

D O I：

10.1073/pnas.95.18.10443

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：10443 / 10448

页数：6

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