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| Domain hiding | Altered binding specificity | Motif hiding | Composite binding site formation |
| Uncategorised | Rheostatic | Allostery | Avidity-sensing |
| Physicochemical compatibility | Pre-translational | Competition |
| Protein | Motif | Start | End | Switch description | Information |
Type: Binary Subtype: Physicochemical compatibility | |||||||
| PTM of a residue in a motif or in its flanking regions alters the physicochemical and/or structural compatibility of the motif with its binding partner. This can either induce or enhance an interaction, or result in inhibition or even abrogation of an interaction. | |||||||
| RARA_HUMAN | DOC_WW_Pin1_4 | 74 | 79 | Phosphorylation of S77 in the Pin1-binding motif of Retinoic acid receptor alpha (RARA) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein. | |||
Type: Binary Subtype: Allostery | |||||||
| The binding properties of a motif or a motif-binding domain are modulated indirectly by allosteric effects resulting from PTM or effector binding at a site that is distinct from the actual interaction interface. | |||||||
| NCOR1_HUMAN | LIG_CORNRBOX | 2051 | 2059 | Binding of the all-trans-retinoic acid ligand to the nuclear Retinoic acid receptor alpha (RARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 1 (NCOR1) inaccessible. | |||
| NCOR1_HUMAN | LIG_CORNRBOX | 2263 | 2271 | Binding of the all-trans-retinoic acid ligand to the nuclear Retinoic acid receptor alpha (RARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 1 (NCOR1) inaccessible. | |||