Receptor binding properties of four‐helix‐bundle growth factors deduced from electrostatic analysis

Hormones of the hematopoietin class mediate signal transduction by binding to specific transmembrane receptors. Structural data show that the human growth hormone (hGH) forms a complex with a homodimeric receptor and that hGH is a member of a class of hematopoietins possessing an antiparallel 4‐α‐helix bundle fold. Mutagenesis experiments suggest that electrostatic interactions may have an important influence on hormone‐receptor recognition. In order to examine the specificity of hormone‐receptor complexation, an analysis was made of the electrostatic potentials of hGH, interleukin‐2 (IL‐2), interleukin‐4 (IL‐4), granulocyte colony‐stimulating factor (G‐CSF), granulocyte‐macrophage colony‐stimulating factor (GM‐CSF), and the hGH and IL‐4 receptors.

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