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Figure 6 | BMC Structural Biology

Figure 6

From: Comparison of tertiary structures of proteins in protein-protein complexes with unbound forms suggests prevalence of allostery in signalling proteins

Figure 6

Normal mode analysis of structural changes in regions of low B-factor away from interface. The protein containing region of interest is depicted as cartoon and the interface of other protein in ribbon. Unbound and bound form of the protein of interest is coloured pale cyan and marine blue, respectively. The partner protein’s unbound and bound forms are coloured light orange and yellow, respectively. Interacting residues are coloured in red and non-interacting residues with PB change in green. All regions of interest are marked with a black circle, irrespective of whether they are intrinsically mobile or rigid. Regions identified to be intrinsically mobile according to NMA are coloured violet. Regions of interest occurring within the intrinsically mobile segments are coloured in dark green. The complexes shown are A). TolB – PAL complex (2HQS) B). Complement C3 and Epstein-Barr virus receptor C2 complex (1GHQ) C). Ran GTPase and Regulator of chromosome condensation (RCC1) complex (1I2M). The partner containing the region of interest is represented in italics. These figures show that noninteracting regions observed to undergo conformational changes upon complexation are usually intrinsically mobile, which is a characteristic of a functional site

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BMC Structural Biology

ISSN: 1472-6807

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