NMR structure of human erythropoietin and a comparison with its receptor bound conformation

被引：135

作者：

Cheetham, JC ^{[1
]}

Smith, DM ^{[1
]}

Aoki, KH ^{[1
]}

Stevenson, JL ^{[1
]}

Hoeffel, TJ ^{[1
]}

Syed, RS ^{[1
]}

Egrie, J ^{[1
]}

Harvey, TS ^{[1
]}

机构：

[1] Amgen Inc, Thousand Oaks, CA 91320 USA

来源：

NATURE STRUCTURAL BIOLOGY | 1998年 / 5卷 / 10期

关键词：

D O I：

10.1038/2302

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The solution structure of human erythropoietin (EPO) has been determined by nuclear magnetic resonance spectroscopy and the overall topology of the protein is revealed as a novel combination of features taken from both the long-chain and short-chain families of hematopoietic growth factors. Using the structure and data from mutagenesis studies we have elucidated the key physiochemical properties defining each of the two receptor binding sites on the EPO protein. A comparison of the NMR structure of the free EPO ligand to the receptor bound form, determined by X-ray crystallography, reveals conformational changes that may accompany receptor binding.

引用

页码：861 / 866

页数：6

共 29 条

[1] ASSOCIATION OF BIOMOLECULAR SYSTEMS VIA PULSED-FIELD GRADIENT NMR SELF-DIFFUSION MEASUREMENTS [J].