Sandbox 27: Difference between revisions
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<Structure load='3g04' size='500' frame='true' align='right' caption='M22 autoantibody complexed with TSHR' scene='Insert optional scene name here' | left /> | <Structure load='3g04' size='500' frame='true' align='right' caption='M22 autoantibody complexed with TSHR' scene='Insert optional scene name here' | left /> | ||
{{STRUCTURE_3g04| PDB=3g04 | SCENE= | size='500'}} | |||
M22 binds to the concave surface of the LRD domain (only a fragment of this domain is represented on the pdb structure: residues 22 to 260 of TSHR) | M22 binds to the concave surface of the LRD domain (only a fragment of this domain is represented on the pdb structure: residues 22 to 260 of TSHR) | ||
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Although the two ligands of TSHR (M22 and TSH) have different structures, there are similar types of interaction. The M22 LC interacts with the LCD in a very close way to the beta-chain of TSH. And it’s the same case with M22 HC and TSH alpha-chain. | Although the two ligands of TSHR (M22 and TSH) have different structures, there are similar types of interaction. The M22 LC interacts with the LCD in a very close way to the beta-chain of TSH. And it’s the same case with M22 HC and TSH alpha-chain. | ||
However we can remark that the M22–TSHR complex involves more strong interactions and fewer hydrophobic interactions than the TSH–TSHR complex. That can explain the effects of the binding of autoantibody like M22 | However we can remark that the M22–TSHR complex involves more strong interactions and fewer hydrophobic interactions than the TSH–TSHR complex. That can explain the effects of the binding of autoantibody like M22. So the idendification of interaction residues and understanding of the mechanism may be useful for developing means of inhibiting TSHR autoantibodies binding. | ||
== Diseases == | == Diseases == | ||