Interleukin-6 (IL-6) is a multifunctional cytokine that regulates cell growth, differentiation, and cellular functions in many cell lineages, Recently, evidences for the formation of an active hexameric complex with an IL-6:IL-6R alpha:gp130 stoichiometry of 2:2:2 have been obtained by different experimental approaches, Analysis of the electrostatic potential complementarity between IL-6 and its receptors has been used, in this study to guide the assembly of homology-based 3D models of the components, The results strongly support a mechanism whereby the active cytokine (IL-6: IL-6R alpha) associates with the signal transducing gp130 protein, and the trimeric complex formed further dimerizes to form the hexameric species. Furthermore, computational simulations of the multiprotein complexes provide a rationalization of data from mutation experiments and highlight some key protein-protein interactions which have not yet been the subject of mutagenesis studies.
Theoretical investigation of IL-6 multiprotein receptor assembly / Menziani, Maria Cristina; Fanelli, Francesca; DE BENEDETTI, Pier Giuseppe. - In: PROTEINS. - ISSN 0887-3585. - STAMPA. - 29:(1997), pp. 528-544. [10.1002/(SICI)1097-0134(199712)29:4<528::AID-PROT12>3.0.CO;2-O]
Theoretical investigation of IL-6 multiprotein receptor assembly
MENZIANI, Maria Cristina;FANELLI, Francesca;DE BENEDETTI, Pier Giuseppe
1997
Abstract
Interleukin-6 (IL-6) is a multifunctional cytokine that regulates cell growth, differentiation, and cellular functions in many cell lineages, Recently, evidences for the formation of an active hexameric complex with an IL-6:IL-6R alpha:gp130 stoichiometry of 2:2:2 have been obtained by different experimental approaches, Analysis of the electrostatic potential complementarity between IL-6 and its receptors has been used, in this study to guide the assembly of homology-based 3D models of the components, The results strongly support a mechanism whereby the active cytokine (IL-6: IL-6R alpha) associates with the signal transducing gp130 protein, and the trimeric complex formed further dimerizes to form the hexameric species. Furthermore, computational simulations of the multiprotein complexes provide a rationalization of data from mutation experiments and highlight some key protein-protein interactions which have not yet been the subject of mutagenesis studies.
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