Zsuzsanna Dosztanyi, Mark Sandor, Peter Tompa and Istvan Simon Pages 161 - 171 ( 11 )
Intrinsically disordered/unstructured proteins exist in a highly flexible conformational state largely devoid of secondary structural elements and tertiary contacts. Despite their lack of a well defined structure, these proteins often fulfill essential regulatory functions. The intrinsic lack of structure confers functional advantages on these proteins, allowing them to adopt multiple conformations and to bind to different binding partners. The structural flexibility of disordered regions hampers efforts solving structures at high resolution by X-ray crystallography and/or NMR. Removing such proteins/ regions from high-throughput structural genomics pipelines would be of significant benefit in terms of cost and success rate. In this paper we outline the theoretical background of structural disorder, and review bioinformatic predictors that can be used to delineate regions most likely to be amenable for structure determination. The primary focus of our review is the interpretation of prediction results in a way that enables segmentation of proteins to separate ordered domains from disordered regions.
Intrinsically unstructured protein, natively unfolded protein, detection of protein disorder, screening disordered protein, target prioritization, high-throughput structural studies, structural genomics
Institute of Enzymology,Biological Research Center, Hungarian Academy of Sciences, Budapest,Hungary, 1518 Budapest, PO Box 7, Hungary.