Classification of intrinsically disordered regions and proteins

Robin Van Der Lee, Marija Buljan, Benjamin Lang, Robert J. Weatheritt, Gary W. Daughdrill, A. Keith Dunker, Monika Fuxreiter, Julian Gough, Joerg Gsponer, David T. Jones, Philip M. Kim, Richard W. Kriwacki, Christopher J. Oldfield, Rohit V. Pappu, Peter Tompa, Vladimir N. Uversky, Peter E. Wright, M. Madan Babu

Research output: Contribution to journalReview article

697 Citations (Scopus)

Abstract

Characterization of unannotated and uncharacterized protein segments is expected to lead to the discovery of novel functions as well as provide important insights into existing biological processes. In addition, it is likely to shed new light on molecular mechanisms of diseases that are not yet fully understood. The classical concept implies that protein sequence defines structure, which in turn determines function; that is, function can be inferred from the sequence and its structure. Even when protein sequences diverge during evolution, for example, after gene duplication, the overall fold of their structures remains roughly the same. Therefore, structural similarity between proteins can reveal distant evolutionary relationships that are not easily detectable using sequence-based methods.

Original languageEnglish
Pages (from-to)6589-6631
Number of pages43
JournalChemical reviews
Volume114
Issue number13
DOIs
Publication statusPublished - Jul 9 2014

ASJC Scopus subject areas

  • Chemistry(all)

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  • Cite this

    Van Der Lee, R., Buljan, M., Lang, B., Weatheritt, R. J., Daughdrill, G. W., Dunker, A. K., Fuxreiter, M., Gough, J., Gsponer, J., Jones, D. T., Kim, P. M., Kriwacki, R. W., Oldfield, C. J., Pappu, R. V., Tompa, P., Uversky, V. N., Wright, P. E., & Babu, M. M. (2014). Classification of intrinsically disordered regions and proteins. Chemical reviews, 114(13), 6589-6631. https://doi.org/10.1021/cr400525m