Protein structure alignment is of importance in protein study. In general, such task can be divided into two categories, i.e. global and local structure alignment. In this paper, one-dimensional features are extracted first from the original protein structures. A hybrid approach combining dynamic time warping and least squares adjustment is proposed for global alignment of protein 3D structures in an iterative fashion, where dynamic time warping is responsible for coarse alignment of two structure and least squares adjustment handles the fine matching of amino acid residues. The residuals of matched pairs are utilized to calculate the weights to accelerate the convergence of coarse-to-fine matching. The preliminary results have demonstrated the effectiveness and efficiency of the proposed approach. However, there is still a room for improvement in terms of accuracy and memory usage.
