A model for hydrophobic protrusions on peripheral membrane proteins
Fig 6
Protruding hydrophobes are found on the membrane binding sites of well known membrane binding domains.
The figure shows the convex hull (in blue) of the Cα and Cβ-atoms of selected peripheral membrane binding domains. The Cβ-atoms of ‘the Likely Inserted Hydrophobe’ are shown as orange spheres and Cβ-atoms of experimentally identified membrane-binding residues as gray spheres. The Likely Inserted Hydrophobe is an amino acid that has been experimentally verified to be a membrane binding residue for A, B, D and F. For C and E the Likely Inserted Hydrophobe is located in the same area as the residues identified by experiments. A: C2 domain of human phospholipase A2 (PDBID: 1RLW [18]); B: PX domain of P40PHOX (PDBID: 1H6H [19]); C: snake phospholipase A2 (PDBID: 1POA [20]); D: C1 domain of protein kinase C δ (PDBID: 1PTR [21]); E: Epsin ENTH domain (PDBID: 1H0A [14]); F: FYVE domain of yeast vacuolar protein sorting-associated protein 27 (PDBID: 1VFY [22]).