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Open Access Highly Accessed Open Badges Methodology article

MICAN : a protein structure alignment algorithm that can handle Multiple-chains, Inverse alignments, C α only models, Alternative alignments, and Non-sequential alignments

Shintaro Minami1, Kengo Sawada2 and George Chikenji1*

Author affiliations

1 Department of Computational Science and Engineering, Nagoya University, Nagoya 464-8603, Japan

2 Department of Applied Physics, Nagoya University, Nagoya 464-8603, Japan

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Citation and License

BMC Bioinformatics 2013, 14:24  doi:10.1186/1471-2105-14-24

Published: 18 January 2013



Protein pairs that have the same secondary structure packing arrangement but have different topologies have attracted much attention in terms of both evolution and physical chemistry of protein structures. Further investigation of such protein relationships would give us a hint as to how proteins can change their fold in the course of evolution, as well as a insight into physico-chemical properties of secondary structure packing. For this purpose, highly accurate sequence order independent structure comparison methods are needed.


We have developed a novel protein structure alignment algorithm, MICAN (a structure alignment algorithm that can handle

ultiple-chain complexes,
nverse direction of secondary structures,
α only models,
lternative alignments, and
on-sequential alignments). The algorithm was designed so as to identify the best structural alignment between protein pairs by disregarding the connectivity between secondary structure elements (SSE). One of the key feature of the algorithm is utilizing the multiple vector representation for each SSE, which enables us to correctly treat bent or twisted nature of long SSE. We compared MICAN with other 9 publicly available structure alignment programs, using both reference-dependent and reference-independent evaluation methods on a variety of benchmark test sets which include both sequential and non-sequential alignments. We show that MICAN outperforms the other existing methods for reproducing reference alignments of non-sequential test sets. Further, although MICAN does not specialize in sequential structure alignment, it showed the top level performance on the sequential test sets. We also show that MICAN program is the fastest non-sequential structure alignment program among all the programs we examined here.


MICAN is the fastest and the most accurate program among non-sequential alignment programs we examined here. These results suggest that MICAN is a highly effective tool for automatically detecting non-trivial structural relationships of proteins, such as circular permutations and segment-swapping, many of which have been identified manually by human experts so far. The source code of MICAN is freely download-able at webcite.