Symmetry in protein complexes
Sergei Grudinin, Guillaume Pagès, David W. Ritchie · 2019
Many protein complexes in the Protein Data Bank (PDB) are symmetric homo-oligomers. Indeed, it appears that large symmetrical protein structures have evolved in many organisms because they carry specific morphological and functional advantages compared to small individual protein molecules. There is therefore considerable interest in studying and modeling these structures. Recently we have proposed a novel free-docking method for protein complexes with arbitrary point-group symmetry. Later on we discovered that the inverse problem, i.e. identification of symmetry in a protein assembly, is even more interesting. Given a structure of the assembly, it consists in the identification of the symmetry measure, and also of the computations of the symmetry axes using geometrical considerations or deep neural networks.