Promiscuous Liaisons: Functional Interactions of Intrinsically Disordered Proteins in Biological Signaling

Event Details
  • Date/Time:
    • Tuesday March 15, 2011 - Wednesday March 16, 2011
      11:00 am - 11:59 am
  • Location: Klaus 1116E
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Jessica Gilmore


Summary Sentence: Peter E. Wright, PhD - Professor and Chair, The Scripps Research Institute

Full Summary: CSSB Distinguished Lecture Series Guest Speaker Peter E. Wright - Professor and Chair, Cecil H. and Ida M. Green Investigator in Biomedical Research, Department of Molecular Biology, The Scripps Research Institute"Promiscuous Liaisons: Functional Interactions of Intrinsically Disordered Proteins in Biological Signaling"

CSSB Distinguished Lecturer Series


Intrinsically disordered proteins participate in important regulatory functions in the cell, including regulation of transcription, translation, the cell cycle, and numerous signal transduction events. Disordered proteins often undergo coupled folding and binding transitions upon interaction with their cellular targets. The lack of stable globular structure can confer numerous functional advantages, including, paradoxically, both binding promiscuity and high specificity in target interactions. NMR is unique in being able to provide detailed insights into the intrinsic conformational preferences and dynamics of unfolded and partly folded proteins, and into the mechanism of coupled folding and binding. The function of intrinsically disordered protein domains in transcriptional regulation and signaling will be described, with particular reference to the general transcriptional coactivators CBP and p300, the tumor suppressor p53, and the adenovirus E1A oncoprotein. The globular domains of CBP/p300 are targets for coupled folding and binding of disordered transactivation motifs of numerous transcription factors and viral oncogenes, which compete for binding to limiting amounts of CBP/p300. Many intrinsically disordered proteins contain multipartite interaction motifs that perform an essential function in the integration of complex signaling networks. The role of multipartite binding motifs and post translational modifications in regulation of p53-mediated signaling pathways will be discussed.

Additional Info:

Dr. Wright's lab uses multidimensional nuclear magnetic resonance (NMR) spectroscopy to investigate the structures, dynamics, and interactions of proteins in solution. Such studies are essential for understanding the mechanisms of action of these proteins and for elucidating structure-function relationships. The focus of their current research is protein-protein and protein-nucleic acid interactions involved in the regulation of gene expression as well as protein folding pathways and enzyme dynamics.

Jeffrey Skolnick - faculty host

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Parker H. Petit Institute for Bioengineering and Bioscience (IBB)

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CSSB, Georgia Tech, Jeffrey Skolnick, Peter E. Wright, Promiscuous Liaisons: Functional Interactions of Intrinsically Disordered Proteins in Biological Signaling
  • Created By: Colly Mitchell
  • Workflow Status: Published
  • Created On: Feb 23, 2011 - 5:05am
  • Last Updated: Oct 7, 2016 - 9:54pm