A model of the ternary complex of interleukin-10 with its soluble receptors |
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Authors: | Sergei?Pletnev Eugenia?Magracheva Alexander?Wlodawer Email author" target="_blank">Alexander?ZdanovEmail author |
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Institution: | (1) Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, MD21702-1201, USA;(2) Basic Research Program, Science Application International Corporation-Frederick, National Cancer Institute at Frederick, Frederick, MD21702-1201, USA |
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Abstract: | Background Interleukin-10 (IL-10) is a cytokine whose main biological function is to suppress the immune response by induction of a signal(s)
leading to inhibition of synthesis of a number of cytokines and their cellular receptors. Signal transduction is initiated
upon formation of a ternary complex of IL-10 with two of its receptor chains, IL-10R1 and IL-10R2, expressed on the cell membrane.
The affinity of IL-10R1 toward IL-10 is very high, which allowed determination of the crystal structure of IL-10 complexed
with the extracellular/soluble domain of IL-10R1, while the affinity of IL-10R2 toward either IL-10 or IL-10/sIL-10R1 complex
is quite low. This so far has prevented any attempts to obtain structural information about the ternary complex of IL-10 with
its receptor chains. |
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