Intrinsically unstructured proteins and their functions

• Published in: Nature reviews. Molecular cell biology Vol. 6; no. 3; pp. 197 - 208
• Main Authors: Wright, Peter E, Dyson, H. Jane
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 01.03.2005
• Subjects: Biology; CREB-Binding Protein; Humans; NMR; Nuclear magnetic resonance; Nuclear Proteins - chemistry; Nuclear Proteins - genetics; Nuclear Proteins - physiology; Nucleic Acids - metabolism; Polypeptides; Protein Binding; Protein Processing, Post-Translational; Protein Structure, Tertiary; Proteins; Proteins - chemistry; Proteins - physiology; Signal transduction; Spectrum analysis; Trans-Activators - chemistry; Trans-Activators - genetics; Trans-Activators - physiology; Tumor Suppressor Protein p53 - chemistry; Tumor Suppressor Protein p53 - physiology
• ISSN: 1471-0072; 1471-0080
• DOI: 10.1038/nrm1589

Many gene sequences in eukaryotic genomes encode entire proteins or large segments of proteins that lack a well-structured three-dimensional fold. Disordered regions can be highly conserved between species in both composition and sequence and, contrary to the traditional view that protein function equates with a stable three-dimensional structure, disordered regions are often functional, in ways that we are only beginning to discover. Many disordered segments fold on binding to their biological targets (coupled folding and binding), whereas others constitute flexible linkers that have a role in the assembly of macromolecular arrays.