Structural Analyses of the Slm1-PH Domain Demonstrate Ligand Binding in the Non-Canonical Site
Figure 6
Structure-based sequence alignment of PH domains of Slm1, β-spectrin and PLCδ.
The alignment was produced using the PROMALS3D program [39] and corrected manually on the basis of the three-dimensional structure of the Slm1-PH. The matched-up sequences were from RCSB/PDB. The secondary structure elements revealed in the Slm1-PH crystal structure are shown above the sequence: β-sheets are shown by blue arrows and the C-terminal helix by an orange cylinder. The residues of Slm1-PH involved in Ins(4)P interaction are shown in red. The residues highlighted in yellow are aligned with the ligand-interacting residues of the Slm1-PH. Residues of different classes of PH domains that are involved in ligand binding are shown in ‘bold’. The R/KXR and R/KXW motifs for ligand binding in the canonical and non-canonical binding sites respectively, are shown in the black box. The structure-based sequence alignment showing overall conserved or semi-conserved residues are represented in grey. Sequences are grouped according to ligand binding in the non-canonical and canonical binding pockets.