Shape complementarity at protein/protein interfaces.

By M. Lawrence, P. Colman. 1993

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Reconfigurable asymmetric protein assemblies through implicit negative design (2021, unknown): “After fusion into cyclic structures, fixed backbone junction design was applied to the new fusion point using RosettaScripts ( 39 ), optimizing for shape complementarity ( 43 ).”
EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. (2003, background): “Moreover, the side chain of a tyrosine (Y246) close to the tip of the domain II -hairpin/ (Lawrence and Colman, 1993) of 0.”
Design of a hyperstable 60-subunit protein icosahedron (2016, unknown): “…optimized using RosettaDesign 20,21 , and 17 designs were selected for experimental characterization based on properties of the designed interface, including shape complementarity 22 , predicted binding energy, and the number of buried unsatisfied hydrogen bond donors and acceptors (see Methods).”
Improving peptide-protein docking with AlphaFold-Multimer using forced sampling (2021, methodology): “…as protein lengths and MSA depths, an updated version of ProQDock (Basu and Wallner, 2016b) was used to calculate the shape complementarity (Sc) (Lawrence and Colman, 1993) and electrostatic complementarity (EC) (McCoy et al., 1997) of native and modelled peptide-protein interfaces; DISOPRED…”