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Figure 3 | BMC Structural Biology

Figure 3

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

Figure 3

Structural changes observed in interfaces. Protein undergoing change is shown as cartoon, with unbound form in light cyan and the bound form in blue, and its partner as a ribbon, with unbound form in light orange and bound form in magenta. Direction of movement is indicated as black arrow. A) Large (~10 Å Cα RMSD) moving out to avoid steric clash (alpha actin & BNI1 protein; 1Y64). B). Movement to optimise interaction with partner (GTP binding protein & Rho GTPase activating protein; 1GRN). C). Conformational change accompanied by movement mainly to avoid steric clashes with the partner (Glycoprotein Ib alpha & von Willebrand factor; 1 M10). In B) and C), the region of interest is colored green and red in the unbound and bound forms, respectively. D). An interface (actin & deoxyribonuclease I; 1ATN) where certain region moves away to avoid steric clash (colored in red), some region undergoes conformational change with movement to optimise an interaction (depicted in green for the unbound form and brown for the bound form) and another region undergoes rigid body movement to optimise its interaction (colored in lemon yellow in the unbound form and orange in the bound form). All the figures containing protein structures were generated using PyMOL [77].

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