结构生物学sturcture biology explore-35.pdfVIP

54 Coupling of folding and binding for unstructured proteins H Jane Dyson* and Peter E Wright† There are now numerous examples of proteins that are Disordered segments appear to be very common in the unstructured or only partially structured under physiological proteins encoded by the various genomes, especially those of conditions and yet are nevertheless functional. Such proteins are higher eukaryotes. A recent survey of 31 genomes indicated especially prevalent in eukaryotes. In many cases, intrinsically that disordered segments longer than 50 residues are highly disordered proteins adopt folded structures upon binding to prevalent [2]. In the four eukaryotic genomes surveyed, their biological targets. Many new examples of coupled folding more than 30% of sequences are predicted to have disordered and binding events have been reported recently, providing new regions of this length and, in Drosophila, a staggering 17% insights into mechanisms of molecular recognition. of proteins are predicted to be wholly disordered. It is probable that coupled folding and binding events will play Addresses an important role in the function of many of these proteins. Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines DNA and RNA binding and transcriptional Road, La Jolla, CA 92037, USA regulation *e-mail: dyson@scripps.edu † e-mail: wright@scripps.edu It has long been recognized that local folding of proteins is frequently coupled to DNA binding [6]. In some