Cheetham J C, Smith D M, Aoki K H, Stevenson J L, Hoeffel T J, Syed R S, Egrie J, Harvey T S
Amgen Inc, Thousand Oaks, California 91320, USA.
Nat Struct Biol. 1998 Oct;5(10):861-6. doi: 10.1038/2302.
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.
人类促红细胞生成素（EPO）的溶液结构已通过核磁共振光谱法确定，该蛋白质的整体拓扑结构显示为造血生长因子长链和短链家族特征的一种新组合。利用该结构和诱变研究数据，我们阐明了定义EPO蛋白上两个受体结合位点各自的关键物理化学性质。将游离EPO配体的核磁共振结构与通过X射线晶体学确定的受体结合形式进行比较，揭示了可能伴随受体结合的构象变化。
