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...
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| Published in | Nature structural biology Vol. 5; no. 10; pp. 861 - 866 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
01.10.1998
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| Subjects | |
| Online Access | Get full text |
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| Abstract | 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. |
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| AbstractList | 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. |
| Author | Stevenson, Janice L Smith, Duncan M Egrie, Joan Cheetham, Janet C Harvey, Timothy S Hoeffel, Thomas J Aoki, Kenneth H Syed, Rashid S |
| Author_xml | – sequence: 1 givenname: Janet C surname: Cheetham fullname: Cheetham, Janet C organization: Amgen Inc – sequence: 2 givenname: Duncan M surname: Smith fullname: Smith, Duncan M organization: Amgen Inc – sequence: 3 givenname: Kenneth H surname: Aoki fullname: Aoki, Kenneth H organization: Amgen Inc – sequence: 4 givenname: Janice L surname: Stevenson fullname: Stevenson, Janice L organization: Amgen Inc – sequence: 5 givenname: Thomas J surname: Hoeffel fullname: Hoeffel, Thomas J organization: Amgen Inc – sequence: 6 givenname: Rashid S surname: Syed fullname: Syed, Rashid S organization: Amgen Inc – sequence: 7 givenname: Joan surname: Egrie fullname: Egrie, Joan organization: Amgen Inc – sequence: 8 givenname: Timothy S surname: Harvey fullname: Harvey, Timothy S organization: Amgen Inc |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9783743$$D View this record in MEDLINE/PubMed |
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| Snippet | The solution structure of human erythropoietin (EPO) has been determined by nuclear magnetic resonance spectroscopy and the overall topology of the protein is... |
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| SubjectTerms | Binding Sites Crystallography, X-Ray Erythropoietin - chemistry Humans Models, Molecular Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Structure, Secondary Receptors, Erythropoietin - chemistry |
| Title | NMR structure of human erythropoietin and a comparison with its receptor bound conformation |
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