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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_PTB_Apo_2 - These phosphorylation-independent motifs bind to Dab-like PTB domains. Binding is not driven by contacts at the 0 or FY position, but instead is dependent upon the large number of hydrophobic and hydrogen bond contacts between motif and domain. | |||||||
| A4_HUMAN | 756 | 763 | Binary | Physicochemical compatibility | Phosphorylation of T743 adjacent to the PTB-binding motif of Amyloid beta A4 protein (APP) reduces the affinity for Amyloid beta A4 precursor protein-binding family B member 1 (APBB1). | ||
| A4_HUMAN | 756 | 763 | Specificity | Altered binding specificity | Phosphorylation of Y757 in APP (Amyloid beta A4 protein (APP)) switches its specificity from PTB domain containing proteins, like Amyloid beta A4 precursor protein-binding family B member 1 (APBB1), which is involved in trafficking and processing of APP, to SH2 domain containing proteins, such as Growth factor receptor-bound protein 2 (GRB2). | ||