Fig. 3: Analysis of VARP residues 692-746:VPS29 interface.
From: Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29
a View of VARP:VPS29 complex rotated from view in Fig. 2 to better show binding surface. b Cut away surface rendering of VPS29 to highlight the hydrophobic pocket in which HisProLeu residues of VARP bind. Key side chains in the interaction are shown and labelled pink (VPS29) or cyan (VARP). c Schematic representation of His, Pro, Leu triplet binding to VPS29. d KDs determined by SPR for mutants in key residues of the VPS29:VARP interface. e Same view as (a) but shown as surface representation with residues whose mutation abolish binding to residues 692-746 of VARP highlighted in red forming a single shallow cavity on the surface of VPS29.
