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A partial model of the erythropoietin receptor complex
Author(s) -
Caravella Justin A.,
Lyne Paul D.,
Richards W. Graham
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199603)24:3<394::aid-prot13>3.0.co;2-h
Subject(s) - erythropoietin , erythropoietin receptor , receptor , homology modeling , haematopoiesis , chemistry , biology , microbiology and biotechnology , genetics , biochemistry , stem cell , enzyme
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.