Shared and unique determinants of the erythropoietin (EPO) receptor are important for binding EPO and EPO mimetic peptide (Q28143503)

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D L Johnson

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R L Thurmond

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Y You

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F J McMahon

6

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R Jin

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O Livnah

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J Tullai

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F X Farrell

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M A Goldsmith

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I A Wilson

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L K Jolliffe

Journal of Biological Chemistry

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language of work or name

English

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publication date

14 May 1999

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published in

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volume

274

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issue

20

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page(s)

14163-9

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Multiple tyrosine residues in the cytosolic domain of the erythropoietin receptor promote activation of STAT5.

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STATs and Gene Regulation

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Haemopoietic receptors and helical cytokines

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Refolding, purification, and characterization of human erythropoietin binding protein produced in Escherichia coli.

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Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 A

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An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation

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Small peptides as potent mimetics of the protein hormone erythropoietin

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Efficiency of signalling through cytokine receptors depends critically on receptor orientation

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Human growth hormone and extracellular domain of its receptor: crystal structure of the complex

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The X-ray structure of a growth hormone-prolactin receptor complex

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Solution structure of an extracellular domain containing the WSxWS motif of the granulocyte colony-stimulating factor receptor and its interaction with ligand

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Crystal structure of a cytokine-binding region of gp130.

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The crystal structure of the extracellular domain of human tissue factor refined to 1.7 A resolution

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Crystal structure of the extracellular region of human tissue factor

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Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor

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Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors

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Identification of a critical ligand binding determinant of the human erythropoietin receptor. Evidence for common ligand binding motifs in the cytokine receptor family

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Identification of a 13 amino acid peptide mimetic of erythropoietin and description of amino acids critical for the mimetic activity of EMP1.

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A single tyrosine residue in the membrane-proximal domain of the granulocyte-macrophage colony-stimulating factor, interleukin (IL)-3, and IL-5 receptor common beta-chain is necessary and sufficient for high affinity binding and signaling by all thr

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Crucial role of the residue R280 at the F'-G' loop of the human granulocyte/macrophage colony-stimulating factor receptor alpha chain for ligand recognition

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The Receptor Binding Site of Human Interleukin-3 Defined by Mutagenesis and Molecular Modeling

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Crystal structure of human interleukin-10 at 1.6 A resolution and a model of a complex with its soluble receptor

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A hot spot of binding energy in a hormone-receptor interface

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Structural and functional epitopes in the growth hormone receptor complex

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A systematic mutational analysis of hormone-binding determinants in the human growth hormone receptor

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Structural design and molecular evolution of a cytokine receptor superfamily

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Quantitation of specific binding of erythropoietin to human erythroid colony-forming cells

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18 Systematic mutational analyses of protein-protein interfaces

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Identification of a Ligand-binding Site on the Granulocyte Colony-stimulating Factor Receptor by Molecular Modeling and Mutagenesis

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Molecular Modeling-guided Mutagenesis of the Extracellular Part of gp130 Leads to the Identification of Contact Sites in the Interleukin-6 (IL-6)·IL-6 receptor·gp130 Complex

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