Sandbox Reserved 971: Difference between revisions
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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. The flexibility of these domains allows ST2 to exist in three different conformers, as you can see on the image below. | 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. The flexibility of these domains allows ST2 to exist in three different conformers, as you can see on the image below. | ||
[[Image:ST2_conformers.png ]] | [[Image:ST2_conformers.png|125px ]] | ||
On the left and on the right, there are respectively the open conformer and the close conformer of ST2. On the middle, the half-open conformer is shown. This conformer superimposes perfectly with the conformation of ST2 bound with IL-33. | On the left and on the right, there are respectively the open conformer and the close conformer of ST2. On the middle, the half-open conformer is shown. This conformer superimposes perfectly with the conformation of ST2 bound with IL-33. | ||
