Low-complexity regions within protein sequences have position-dependent roles |
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| Authors: | Alain Coletta John W Pinney David Y Weiss Solís James Marsh Steve R Pettifer Teresa K Attwood |
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| Institution: | 1.Faculty of Life Sciences,University of Manchester,Manchester,UK;2.School of Computer Science,University of Manchester,Manchester,UK;3.Department of Applied Biological Sciences, Switch Laboratory,Vrije Universiteit Brussel,Belgium;4.Division of Molecular Biosciences,Centre for Bioinformatics, Imperial College London,London,UK;5.Institute of Interdisciplinary Research (IRIBHM), School of Medicine,Free University of Brussels,Brussels,Belgium;6.IRIDIA-CoDE,Université Libre de Bruxelles,Brussels,Belgium |
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| Abstract: | Background Regions of protein sequences with biased amino acid composition (so-called Low-Complexity Regions (LCRs)) are abundant in
the protein universe. A number of studies have revealed that i) these regions show significant divergence across protein families;
ii) the genetic mechanisms from which they arise lends them remarkable degrees of compositional plasticity. They have therefore
proved difficult to compare using conventional sequence analysis techniques, and functions remain to be elucidated for most
of them. Here we undertake a systematic investigation of LCRs in order to explore their possible functional significance,
placed in the particular context of Protein-Protein Interaction (PPI) networks and Gene Ontology (GO)-term analysis. |
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