Proteins without 3D structure: definition, detection and beyond

Bioinformatics. 2011 Jun 1;27(11):1449-54. doi: 10.1093/bioinformatics/btr175. Epub 2011 Apr 14.

Abstract

Predictions, and experiments to a lesser extent, following the decoding of the human genome showed that a significant fraction of gene products do not have well-defined 3D structures. While the presence of structured domains traditionally suggested function, it was not clear what the absence of structure implied. These and many other findings initiated the extensive theoretical and experimental research into these types of proteins, commonly known as intrinsically disordered proteins (IDPs). Crucial to understanding IDPs is the evaluation of structural predictors based on different principles and trained on various datasets, which is currently the subject of active research. The view is emerging that structural disorder can be considered as a separate structural category and not simply as absence of secondary and/or tertiary structure. IDPs perform essential functions and their improper functioning is responsible for human diseases such as neurodegenerative disorders.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Humans
  • Protein Conformation*
  • Protein Folding
  • Proteins / chemistry
  • Proteins / metabolism

Substances

  • Proteins