Intrinsically unstructured proteins and their functions.
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.
Dyson
H Jane
HJ
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA. dyson@scripps.edu
Wright
Peter E
PE
D050882:CREB-Binding Protein; D006801:Humans; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D009696:Nucleic Acids / Q000378:metabolism; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000502:physiology*; D015534:Trans-Activators / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000502:physiology
D009687:Nuclear Proteins; D009696:Nucleic Acids; D011506:Proteins; D015534:Trans-Activators; D016159:Tumor Suppressor Protein p53; D050882:CREB-Binding Protein; C494363:CREBBP protein, human