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Figure 7 | BMC Biochemistry

Figure 7

From: Binding to DPF-motif by the POB1 EH domain is responsible for POB1-Eps15 interaction

Figure 7

Structural analysis of the NPF-binding pocket of Eps15 (EH2) and POB1 EH domain. Molecular surface representations of the NPF-binding pocket of the Eps15 EH2, PDB code: 1EH2 (A), Eps15 EH1, PDB code: 1QJT (B) and POB1, PDB code: 1IQ3 (C) EH domains. Residues in the hydrophobic groove are coloured in red, residues which line the edge of the binding pocket are in green while the gate charged residues are in blue. (B) Left panel: representation of the classical binding pocket of Eps15 EH1 domain. Right panel: residues distant from the binding pocket, which have been discussed in the text, are mapped on the molecular surface of Eps15. Lys 21 indicates the position of the binding pocket. (C) Left panel: representation of the classical binding pocket of POB1 EH domain. Right panel: residues mutated in this study are mapped on the molecular surface of POB1. Lys 307 indicates the position of the binding pocket. Lysine residues are coloured in blue, Phe344 and Ile347 in red and Gln289 in orange. Molecular surfaces were generated with PyMol.

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