The interleukin-6 (IL-6) partial antagonist (Q159E,T162P)IL-6 interacts with the IL-6 receptor and gp130 but fails to induce a stable hexameric receptor complex.

作者: Annet Hammacher , Richard J. Simpson , Edouard C. Nice

DOI: 10.1074/JBC.271.10.5464

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摘要: Abstract The extracellular “soluble” domains of the IL-6 receptor (sIL-6R) and gp130 (sgp130) form a hexameric ternary complex together with IL-6, consisting two molecules each component. In this report we have investigated interactions partial antagonist (Q159E,T162P)IL-6 ((QT)IL-6), sIL-6R sgp130. kinetic rate constants binding to immobilized monomeric (QT)IL-6 or were obtained using an optical biosensor analysis primary data by linear nonlinear regression. Both methods showed that, due higher off-rate, has lower apparent affinity for than IL-6. was further confirmed equilibrium measurements at sensor surface in solution. Using it also shown that interacts sgp130, supporting notion biological activity is mediated via gp130. However, mutant, when incubated failed induce stable complex, as narrowbore size exclusion chromatography.

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