Disordered regions (DRs) are entire proteins or regions of proteins which lack a fixed tertiary structure, essentially being partially or fully unfolded. Such disordered regions have been shown to be involved in a variety of functions, including DNA recognition, modulation of specificity/affinity of protein binding, molecular threading, activation by cleavage, and control of protein lifetimes. Although these DRs lack a defined 3-D structure in their native states, they frequently undergo disorder-to-order transitions upon binding to their partners.
Documentation, Other Resources
Romero, P., Z. Obradovic, C.R. Kissinger, J.E. Villafranca, and A.K. Dunker (1997) Identifying Disordered Regions in Proteins from Amino Acid Sequences.
Proc. I.E.E.E. International Conference on Neural Networks, p. 90-95.
Last modified: 12/30/06