Figure 6.

Sequence conservation within the actin binding region. The sequence logos illustrate the sequence conservation within the multiple sequence alignments of the coronin domains. Here, only the N- and C-termini of the coronin domains are shown because most of the residues implicated in actin binding map to these regions. For the representation of the entire coronin domain see Additional file 5. For better orientation, the sequences of three representative coronins are shown: the yeast coronin as the main target of mutagenesis experiments, the Dictyostelium coronin as the founding member of the protein family, and the murine coronin-1A of which the crystal structure is known. Secondary structural elements as determined from the crystal structure are drawn as yellow arrows (β-strands) and red boxes (α-helices). Green dots point to amino acids of ScCoro that have been mutated to alanine [41] and red dots highlight mutagenesis studies in HsCoro1B [40]. Light-blue boxes highlight mutations that abolished actin binding, dark-grey boxes represent mutations that did not influence actin binding, and light-grey boxes point to mutations in yeast coronins that could not be expressed and tested.

Eckert et al. BMC Evolutionary Biology 2011 11:268   doi:10.1186/1471-2148-11-268
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