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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: Specificity Subtype: Domain hiding | |||||||
| A domain can be sterically masked by binding of an effector when there is a large difference in intrinsic affinity of the domain for different binding partners, or a large difference in the local abundance of these partners, thereby precluding further interactions of the domain. Binding of the masking molecule can be PTM-dependent or -independent. | |||||||
| GRM5_RAT | LIG_PDZ_Class_1 | 1198 | 1203 | Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin (Grasp) PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin (Grasp) PDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (Grasp) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details. | |||
| GRASP_RAT | LIG_PDZ_Class_1 | 389 | 394 | Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin (Grasp) PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin (Grasp) PDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (Grasp) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details. | |||
Type: Specificity Subtype: Motif hiding | |||||||
| Motif hiding occurs when there is a large difference in intrinsic affinity of overlapping or adjacent motifs for their respective binding partners, or a large difference in the local abundance of these partners. Binding of an effector to one motif sterically masks the overlapping or adjacent motif, thereby precluding it from binding. Binding of the masking molecule can be PTM-dependent or -independent. | |||||||
| GRASP_RAT | LIG_PDZ_Class_1 | 389 | 394 | Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin Grasp PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin GraspPDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (General receptor for phosphoinositides 1-associated scaffold protein (Grasp)) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details. | |||
| GRASP_RAT | LIG_PDZ_Class_1 | 389 | 394 | Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin Grasp PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin GraspPDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (General receptor for phosphoinositides 1-associated scaffold protein (Grasp)) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details. | |||