Sandbox 27: Difference between revisions
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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) | ||
The binding results of several interactions between TSHR and M22, most of them are hydrogen bonds and salt bridges. The <scene name='Sandbox_27/Chaine_b/3'>heavy chain</scene> (HC, or Chain B) of M22 has more interactions with the <scene name='Sandbox_27/Chaine_c/1'>LRD</scene> than has the <scene name='Sandbox_27/Chaine_a/2'>light chain</scene> (LC, or Chain A), respectively 14 and 8 interactions. | The binding results of several interactions between TSHR and M22, most of them are hydrogen bonds and salt bridges. The <scene name='Sandbox_27/Chaine_b/3'>heavy chain</scene> (HC, or Chain B) of M22 has more interactions with the <scene name='Sandbox_27/Chaine_c/1'>LRD</scene> than has the <scene name='Sandbox_27/Chaine_a/2'>light chain</scene> (LC, or Chain A), respectively 14 and 8 interactions. | ||
The binding of M22 to the LRD must induce changes in the receptor conformation, which cause signal induction, but the nature of these changes are not currently known. Indeed no movement of the atoms of M22 is observed after its binding to the receptor. This conformational change may occur also with TSH binding. | The binding of M22 to the LRD must induce changes in the receptor conformation, which cause signal induction, but the nature of these changes are not currently known. Indeed no movement of the atoms of M22 is observed after its binding to the receptor. This conformational change may occur also with TSH binding. | ||
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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. ([[Diseases]]). So the idendification of interaction residues and understanding of the mechanism may be useful for developing means of inhibiting TSHR autoantibodies binding. | 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. ([[Diseases]]). So the idendification of interaction residues and understanding of the mechanism may be useful for developing means of inhibiting TSHR autoantibodies binding. | ||
== Diseases == | == Diseases == | ||