Review
Nature Reviews Molecular Cell Biology 6, 197-208 (March 2005) | doi:10.1038/nrm1589
Intrinsically unstructured proteins and their functions
H. Jane Dyson1 & Peter E. Wright1 About the authors
Abstract
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.
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Author affiliations
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Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Email: dyson@scripps.edu
Email: wright@scripps.edu
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