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Propensity; structure–function correlation; human genome; structural plasticity; three-dimensional structure; identical and similar sequence repeats

Amino acid sequences are known to constantly mutate and diverge unless there is a limiting condition that makes such a change deleterious. However, closer examination of the sequence and structure reveals that a few large, cryptic repeats are nevertheless sequentially conserved. This leads to the question of why only certain repeats are conserved at the sequence level. It would be interesting to find out if these sequences maintain their conservation at the three-dimensional structure level. They can play an active role in protein and nucleotide stability, thus not only ensuring proper functioning but also potentiating malfunction and disease. Therefore, insights into any aspect of the repeats – be it structure, function or evolution – would prove to be of some importance. This study aims to address the relationship between protein sequence and its three-dimensional structure, by examining if large cryptic sequence repeats have the same structure.

R Sarani¹ N A Udayaprakash¹ R Subashini¹ P Mridula¹ T Yamane² K Sekar^{1 3}

1. Bioinformatics Centre, Indian Institute of Science, Bangalore 560 012, India
2. Department of Biotechnology, Graduate School of Engineering, Nagoya University, Furo-cho, Nagoya 464-8603, Japan
3. Supercomputer Education and Research Centre, Indian Institute of Science, Bangalore 560 012, India

Published

March 2009

Manuscript received

16 June 2008

Accepted

12 December 2008

Early published

29 January 2009