Caravella J A, Lyne P D, Richards W G
Physical and Theoretical Chemistry Laboratory, Oxford University, United Kingdom.
Proteins. 1996 Mar;24(3):394-401. doi: 10.1002/(SICI)1097-0134(199603)24:3<394::AID-PROT13>3.0.CO;2-H.
A model of the structure of erythropoietin (Epo) is presented based on structural homology to other hemopoietic cytokines. A model of the erythropoietin receptor complex was made based on evidence that this includes a homodimer of the receptor chain with known sequence. Key interactions are noted which explain data from mutation experiments, although at not all residues believed to be important to binding of Epo are at the interface. This is consistent with the hypothesis that the Epo receptor complex includes proteins in addition to the cloned receptor chain that have been cross-linked to Epo (Todokoro et al., Proc. Natl. Acad. Sci. USA 84:4126-4130, 1987; Mayeux et al., J. Biol. Chem. 266:23380-23385, 1991) but not isolated.
