Sandbox Reserved 971: Difference between revisions
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In the complex, IL-33 interacts with the three domains of ST2. The binding interface is very large and composed of two separate sites. | In the complex, IL-33 interacts with the three domains of ST2. The binding interface is very large and composed of two separate sites. | ||
In the <scene name='61/614056/Interaction_site_1/7'>first binding site</scene>, thirteen IL-33 residues from β-loops are in contact with the D1D2 module of ST2: the four marked acids residues of IL-33 form a salt-bridge with five marked ST2 residues respectively. Besides, | In the <scene name='61/614056/Interaction_site_1/7'>first binding site</scene>, thirteen IL-33 residues from β-loops are in contact with the D1D2 module of ST2: the four marked acids residues of IL-33 form a salt-bridge with five marked ST2 residues respectively. Besides, <scene name='61/614056/Il3_and_st2_with_two_colors/4'>Glu 144 and Asp149</scene> form hydrogen bonds with main-chain atoms of ST2. IL-33 mutation of one of the acid residues (144, 148, 149 and 244) highly decreases the affinity of ST2 for IL-33. | ||
In the <scene name='61/614056/Interaction_site_2/3'>second binding site</scene>, eight IL-33 residues from β-strands interact with the D3 domain of ST2. | In the <scene name='61/614056/Interaction_site_2/3'>second binding site</scene>, eight IL-33 residues from β-strands interact with the D3 domain of ST2. | ||
