Sandbox Reserved 971: Difference between revisions
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The understanding of the interaction of IL-33 with its receptors has been discovered thanks to the determination of the crystal structure of IL-33 in complex with ectodomain of ST2. | The understanding of the interaction of IL-33 with its receptors has been discovered thanks to the determination of the crystal structure of IL-33 in complex with ectodomain of ST2. | ||
Besides, the combination of crystallography and small-angle X-ray-scattering methods reveal that ST2 has a very flexible conformation, contrary to IL-1RAcP. In fact, ST2 is constituted of three IgG-like domains (<scene name='61/614056/Domains_d1d2d3_de_st2/1'>D1 to D3</scene>). D1 and D2 gather to form a single D1D2 module, connected through a linker with the D3 domain. ST2 contains also < | Besides, the combination of crystallography and small-angle X-ray-scattering methods reveal that ST2 has a very flexible conformation, contrary to IL-1RAcP. In fact, ST2 is constituted of three IgG-like domains (<scene name='61/614056/Domains_d1d2d3_de_st2/1'>D1 to D3</scene>). D1 and D2 gather to form a single D1D2 module, connected through a linker with the D3 domain. ST2 contains also <scene name='61/614056/Three_residues_of_st2_with_nag/3'>three residues</scene> linked with NAG and an <scene name='61/614056/St2_hydrophobic_patch/1'>hydrophobic patch</scene> which is involved in the interaction with the other receptor, IL-1RAcP. | ||
This conformational specificity provides a capactity of ligand-binding with IL-33. Moreover, the rigidity of IL-1RAcP explains that it can not bind the IL-33 ligand directly. | This conformational specificity provides a capactity of ligand-binding with IL-33. Moreover, the rigidity of IL-1RAcP explains that it can not bind the IL-33 ligand directly. | ||
