Structural and functional basis for hormone binding and receptor oligomerization.
Most single-pass transmembrane receptors undergo a change in oligomeric state upon hormone binding. Recent mutational, biophysical and structural studies of the human growth hormone and tumor necrosis factor receptor complexes have revealed much about the mechanisms and molecular bases for binding and oligomerization. Principles learned from these examples and others should apply to many other hormone-receptor complexes.
Department of Protein Engineering, Genentech, Inc., South San Francisco, CA 94080.
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D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D016207:Cytokines / Q000737:chemistry / Q000378:metabolism; D013006:Growth Hormone / Q000737:chemistry / Q000378:metabolism; D006728:Hormones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008563:Membrane Lipids / Q000378:metabolism; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism*; D018121:Receptors, Cytokine / Q000737:chemistry / Q000378:metabolism; D011986:Receptors, Somatotropin / Q000737:chemistry / Q000378:metabolism; D018124:Receptors, Tumor Necrosis Factor / Q000737:chemistry / Q000378:metabolism; D014409:Tumor Necrosis Factor-alpha / Q000737:chemistry / Q000378:metabolism
D016207:Cytokines; D006728:Hormones; D008563:Membrane Lipids; D011956:Receptors, Cell Surface; D018121:Receptors, Cytokine; D011986:Receptors, Somatotropin; D018124:Receptors, Tumor Necrosis Factor; D014409:Tumor Necrosis Factor-alpha; D013006:Growth Hormone