Structural-symmetry-related sequence patterns of the proteins of beta-propeller family

It is still not very clear to what extent and how does the amino acid sequences of proteins determine their tertiary structures. In this paper, we report our investigations of the sequence–structure relations of the proteins in the beta-propeller fold family, which adopt highly symmetrical tertiary structures while their sequences appear “random”. We analyzed the amino acid sequences by using a similarity matrix plus Pearson correlation method and found that the sequences can show the same symmetries as their tertiary structures only if we deduce the conditions of sequence similarity. This suggests that some key residues may play an important role in the formation of the tertiary structures of these proteins.