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

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 th...

Full description

Saved in:
Bibliographic Details
Published inNature structural biology Vol. 5; no. 10; pp. 861 - 866
Main Authors Cheetham, Janet C, Smith, Duncan M, Aoki, Kenneth H, Stevenson, Janice L, Hoeffel, Thomas J, Syed, Rashid S, Egrie, Joan, Harvey, Timothy S
Format Journal Article
LanguageEnglish
Published United States 01.10.1998
Subjects
Binding Sites
Crystallography, X-Ray
Erythropoietin - chemistry
Humans
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Protein Structure, Secondary
Receptors, Erythropoietin - chemistry
Online AccessGet full text

Cover

More Information
Summary: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.
ISSN:1072-8368
2331-365X
DOI:10.1038/2302