| Autor: |
Cheetham JC; Amgen Inc, Thousand Oaks, California 91320, USA. cheetham@amgen.com, Smith DM, Aoki KH, Stevenson JL, Hoeffel TJ, Syed RS, Egrie J, Harvey TS |
| Jazyk: |
angličtina |
| Zdroj: |
Nature structural biology [Nat Struct Biol] 1998 Oct; Vol. 5 (10), pp. 861-6. |
| DOI: |
10.1038/2302 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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