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- W2491534819 abstract "The gp130-cytokine system has been the subject of extensive protein structure-function studies aimed at elucidating the basis of ligand recognition and receptor activation. A longstanding question has been the architecture of the higher order signaling assembly. It is clear from functional studies that the paradigm of gp130-cytokine recognition will differ substantially from the classical homodimeric systems typified by human growth hormone and its receptor. Recently, the crystal structure of a viral interleukin-6 (IL-6) complexed with the D1, D2, and D3 domains of the gp130 extracellular domain has reconciled much of the functional and mutagenesis data that exist for a variety of gp130-cytokine systems. The topology of the viral IL-6-gp130 assembly also appears to satisfy the structural requirements of an analogous signaling complex of granulocyte colony-stimulating factor (GCSF) and its receptor. A previous crystal structure of an “inactive” form of this complex can be supplanted by a new model incorporating known functional data implicating the N-terminal immunoglobulin (Ig)-like domain of the GCSF receptor as the key to assembling an interlocking tetramer, as seen in gp130-cytokines." @default.
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- W2491534819 date "2003-01-01" @default.
- W2491534819 modified "2023-09-23" @default.
- W2491534819 title "A New Paradigm of Cytokine Action Revealed by Viral IL-6 Complexed to gp130: Implications for GCSF Interaction with GCSFR" @default.
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- W2491534819 doi "https://doi.org/10.1016/b978-012124546-7/50405-8" @default.
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