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TitleAn antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation.
Journal, issue, pagesNat. Struct. Biol., Vol. 5, Page 993-1004, Year 1998
Publish dateOct 2, 1998 (structure data deposition date)
AuthorsLivnah, O. / Johnson, D.L. / Stura, E.A. / Farrell, F.X. / Barbone, F.P. / You, Y. / Liu, K.D. / Goldsmith, M.A. / He, W. / Krause, C.D. ...Livnah, O. / Johnson, D.L. / Stura, E.A. / Farrell, F.X. / Barbone, F.P. / You, Y. / Liu, K.D. / Goldsmith, M.A. / He, W. / Krause, C.D. / Pestka, S. / Jolliffe, L.K. / Wilson, I.A.
External linksNat. Struct. Biol. / PubMed:9808045
MethodsX-ray diffraction
Resolution2.7 Å
Structure data

PDB-1eba:
COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / ERYTHROPOIETIN RECEPTOR / SIGNAL TRANSDUCTION / PROTEIN MINIMIZATION / DRUG DESIGN / CYTOKINE RECEPTOR CLASS 1 / COMPLEX (CYTOKINE RECEPTOR-PEPTIDE)

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