Different Modes of Inhibitor Binding to Prolyl Hydroxylase by Combined Use of X-ray Crystallography and NMR Spectroscopy of Paramagnetic Complexes

被引：21

作者：

Poppe, Leszek ^{[1
]}

Tegley, Christopher M.

Li, Vivian ^{[1
]}

Lewis, Jeffrey

Zondlo, James

Yang, Evelyn

Kurzeja, Robert J. M.

Syed, Rashid ^{[1
]}

机构：

[1] Amgen Inc, Dept Mol Struct, Thousand Oaks, CA 91320 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 46期

关键词：

PROTEINS;

D O I：

10.1021/ja907933p

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

In aqueous solution, azaquinolone inhibitors bind to prolyl 4-hydroxylase in two different orientations, as first detected by (19)F spectroscopy. This contrasts with the crystallographic structure where only one orientation has been determined. Dissection of the metal binding properties of the enzyme allowed structures of both complexes to be obtained in solution from (19)F and (13)C dipolar shifts in a labeled ligand.

引用

页码：16654 / +

页数：4

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