Figure 9

Structural analysis of activity essential regions of TcAkt and HsAkt1. Due to high differences in the residual arrangements the structures are not superimposed. HsAkt PH domain is shown in green, HsAkt kinase domain in blue and the C-tail in grey. TcAkt PH domain is shown in turquoise, TcAkt kinase domain in sand and the C-tail in lavender. Flexible interdomain linkers are shown in light grey. PIP binding site: (a) PIP binding site of HsAkt1: PIP interacting residues are shown as green sticks (derived from the crystal structure of HsAkt1-PH in complex with Ins(1,3,4,5)P₄ ;PDB: 1UNQ) and presented on the apo structure (PDB: 1UNP) for comparative reasons. (b) PIP binding site of TcAkt: PIP interacting residues are shown as turquoise sticks (derived from NMR analysis and MD simulations) and presented on the apo structure (PDB: 8OZZ). Intramolecular interface: (c) Intramolecular interface of HsAkt1 as zoomed detail from full-length HsAkt1 (PDB: 7APJ): Involved residues of the kinase (HsAkt1-K: blue) and the PH domain (HsAkt1-PH: green) are shown as sticks. (d) Intramolecular interface of TcAkt as zoomed detail from full-length TcAkt (AF model): Involved residues of  the kinase (HsAkt1-K: sand) and the PH domain (HsAkt1-PH: turquoise) are shown as sticks. Conserved residues are marked with an asterisk (*).