TAILIEUCHUNG - Báo cáo khoa học: Protein tandem repeats – the more perfect, the less structured

We analysed the structural properties of protein regions containing arrays of perfect and nearly perfect tandem repeats. Naturally occurring proteins with perfect repeats are practically absent among the proteins with known 3D structures. The great majority of such regions in the Protein Data Bank are found in the proteins designed de novo. | ỊFEBS Journal Protein tandem repeats - the more perfect the less structured Julien Jorda1 Bin Xue2 3 Vladimir N. Uversky2 3 4 5 and Andrey V. Kajava1 1 Centre de Recherches de Biochimie Macromoleculaire CNRS UMR-5237 University of Montpellier 1 and 2 France 2 Center for ComputationalBiology and Bioinformatics Indiana University Schoolof Medicine Indianapolis IN USA 3 Institute for Intrinsically Disordered Protein Research Indiana University Schoolof Medicine Indianapolis IN USA 4 Institute for BiologicalInstrumentation Russian Academy of Sciences Pushchino Moscow Region Russia 5 Department of Biochemistry and Molecular Biology Indiana University Schoolof Medicine Indianapolis IN USA Keywords bioinformatics disordered conformation evolution protein structure sequence analysis Correspondence A. V. Kajava Centre de Recherches de Biochimie Macromoleculaire CNRS 1919 Route de Mende 34293 Montpellier Cedex 5 France Fax 33 4 67 521559 Tel 33 4 67 61 3364 E-mail Received 23 February 2010 revised 7 April 2010 accepted 12 April 2010 doi We analysed the structural properties of protein regions containing arrays of perfect and nearly perfect tandem repeats. Naturally occurring proteins with perfect repeats are practically absent among the proteins with known 3D structures. The great majority of such regions in the Protein Data Bank are found in the proteins designed de novo. The abundance of natural structured proteins with tandem repeats is inversely correlated with the repeat perfection the chance of finding natural structured proteins in the Protein Data Bank increases with a decrease in the level of repeat perfection. Prediction of intrinsic disorder within the tandem repeats in the Swiss-Prot proteins supports the conclusion that the level of repeat perfection correlates with their tendency to be unstructured. This correlation is valid across the various species and subcellular localizations although the level of

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