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Symmetry is a common and significant feature of protein structures. Symmetry has been found to be important for understanding protein evolution, DNA binding, allosteric regulation, cooperativity, and folding. We have compiled a census of internal symmetry, conducted using the novel CE-Symm algorithm. We find that internal symmetry is present in at least 18% of superfamilies. To elucidate the relationship between symmetry and protein function, the census is analyzed with respect to structural classification, enzyme activity, and ligand binding. The CE-Symm algorithm was benchmarked against a manually curated set of ~1000 domains.
Myers-Turnbull, D., Bliven, S. E., Rose, P. W., Aziz, Z. K., Youkharibache, P., Bourne, P. E., & Prlić, A. (2014). Systematic Detection of Internal Symmetry in Proteins Using CE-Symm. Journal of Molecular Biology, 426(11), 2255–2268. PMID: 24681267
This poster was presented at the 22nd Annual International Conference on Intelligent Systems for Molecular Biology (2014).