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- W2367669387 abstract "Interleukin-6 receptor (IL-6R) is a member of the hematopoietin receptor superfamily which has its common conservative structure “the cytokine binding domain (CBD)”. CBD is the functional domain of the extracellular region of IL-6R, because only this domain of IL-6R is responsible for IL-6-binding and for IL-6 signal transduction through gp130. It is proposed that the β-sheets folding motif of the IL-6R CBD is very similar to that seen in the crystal structure of human growth hormone receptor (hGH-R), which also belongs to the cytokine receptor fam- ily, and CD4. By means of computer-guided homology modeling techniques, the three- dimensional (3D) structures of hGH-R and CD 4 were used as template protein to predict the 3D-structure of the functional domain (residue 106～322) of hIL-6R. The characteristics of the conservative structure-conformation in CBD of hIL-6R were described. The model may provide for the interpretation of the results obtained with introducing site-directed mutation into soluble IL-6R and the 3D-quantitative analysis on the structure-function relationship of IL-6R functional domain." @default.
- W2367669387 created "2016-06-24" @default.
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- W2367669387 date "1997-01-01" @default.
- W2367669387 modified "2023-09-27" @default.
- W2367669387 title "Homology Modeling of the Functional Domain of the Extracellular Region of Human IL-6 Receptor" @default.
- W2367669387 hasPublicationYear "1997" @default.
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