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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 | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
LIG_PDZ_Class_1 - The C-terminal class 1 PDZ-binding motif is classically represented by a pattern like (ST)X(VIL)* | |||||||
| ADRB2_HUMAN | 408 | 413 | Binary | Physicochemical compatibility | Phosphorylation of S411 in the PDZ-binding motif of Beta-2 adrenergic receptor (ADRB2) by inhibits its interaction with the Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) protein. | ||
| CTNB1_HUMAN | 776 | 781 | Binary | Allostery | Binding of Ezrin (EZR) via its FERM domain to the EB domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) results in allosteric coupling to the second PDZ domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1), which results in relief of the intramolecular interaction with the PDZ binding ligand, thereby increasing the affinity of the PDZ domain for other ligands, including Catenin beta-1 (CTNNB1). | ||
| NHRF1_HUMAN | 353 | 358 | Specificity | Domain hiding | Binding of Ezrin via its FERM domain to the EB domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) results in allosteric coupling to the second PDZ domain of SLC9A3R1. This relieves the intramolecular interaction with the SLC9A3R1 PDZ-binding ligand and increases the affinity of the PDZ domain for other ligands including Catenin beta-1 (CTNNB1). | ||
| CTNB1_HUMAN | 776 | 781 | Specificity | Domain hiding | Binding of Ezrin via its FERM domain to the EB domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) results in allosteric coupling to the second PDZ domain of SLC9A3R1. This relieves the intramolecular interaction with the SLC9A3R1 PDZ-binding ligand and increases the affinity of the PDZ domain for other ligands including Catenin beta-1 (CTNNB1). | ||
| CFTR_HUMAN | 1475 | 1480 | Specificity | Competition | The PDZ domains of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) and SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) compete for the PDZ-binding motif of Cystic fibrosis transmembrane conductance regulator (CFTR). SLC9A3R1 positively regulates CFTR activity by recruiting a PKA-containing complex, while SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) negatively affects CFTR activity by recruiting PDE4D. | ||
| CFTR_HUMAN | 1475 | 1480 | Specificity | Competition | The PDZ domains of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) and SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) compete for the PDZ-binding motif of Cystic fibrosis transmembrane conductance regulator (CFTR). SLC9A3R1 positively regulates CFTR activity by recruiting a PKA-containing complex, while SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) negatively affects CFTR activity by recruiting PDE4D. | ||
| CLCN3_HUMAN | 861 | 866 | Binary | Pre‑translational | Alternative splicing removes the PDZ-binding motif of Isoform ClC-3B of H(+)/Cl(-) exchange transporter 3 (CLCN3), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1). Isoform ClC-3B of H(+)/Cl(-) exchange transporter 3 (CLCN3) is expressed at the leading edge of membrane ruffles. The interaction of CLCN3 with SLC9A3R1 is important for localising outwardly rectifying chloride channels at the leading edge. | ||
| PGFRB_HUMAN | 1101 | 1106 | Binary | Physicochemical compatibility | Phosphorylation of S1104 in the PDZ-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) by Beta-adrenergic receptor kinase 1 (ADRBK1) inhibits binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1). Binding of Platelet-derived growth factor receptor beta (PDGFRB) to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) potentiates dimerisation and signalling of the receptor, while phosphorylation at S1104 desensitises the receptor. | ||