Fig. 2: Structure of the VARP 692–746:VPS29 complex.
From: Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29
a Histogram showing chemical shift perturbation (CSP) values for the amide group signals of 15N labelled VPS29 on binding of VARP residues 692–746 calculated according to the equation CSP = (Δδ(1H)2 + 0.2(Δδ(15N)2))0.5; the largest CSP value is 0.662 (for Leu 26) and is truncated in this plot. The bar to the right of the plot shows the colour code used to map these CSP values to the structure: values between 0 and 0.331 (half the largest CSP value) are shown using a colour ramp running from grey to yellow, while values >0.331 are uniformly shown as yellow. b Mapping of the CSP data onto the structural model of the complex of VPS29 with VARP 692–746, using the colour ramp defined in panel a). Only the ordered residues (709–721) of the VARP fragment are shown. c, d VPS29 coloured from N (pink) to C (dark red), together with the ordered residues (709–721) of the VARP fragment coloured from N (pale cyan) to C (deep cyan) with cysteine side chains shown and the Zn++ atom indicated by a grey sphere. c shows the ‘family’ of 25 best fit structures of the complex and d shows the lowest energy structure. e Enlargement of the ordered residues (709–721) of the VARP fragment taken from the lowest energy structure of the complex; key residues are indicated.
