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Fuzzy complexes: ambiguity in protein-protein and protein-DNA interactions

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  • UserProfessor Monika Fuxreiter Institute of Enzymology, Budapest, HUNGARY and LMB, MRC, Cambridge, UK
  • ClockWednesday 16 November 2011, 10:15-11:15
  • HousePerham's seminar room.

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For a long time, protein function was thought to be determined by a well-defined three-dimensional structure. Recently it has been realized however, that many proteins disobey this classical structure-function paradigm. Intrinsically disordered (ID) proteins function as multiplicity of structures and their activities can only be described by stochastic structure-function relationships. In their complex forms however, ID proteins were thought to loose their plasticity and behave similarly to globular proteins. Although various ID regions indeed fold upon binding, this view is not valid in general. ID segments usually interact with their partners via short motifs, which require malleable environments to function. Consequently, ID regions could retain their disordered state in the complex, a phenomenon termed as fuzziness. The number of structurally characterized fuzzy complexes, both with protein and DNA , rapidly increases. I describe four molecular mechanisms how conformationally heterogeneous regions impact specificity or binding affinity of protein-protein and protein-DNA complexes. In these cases the regulatory sites modulate the conformational equilibrium of the binding interface without adopting a unique structure. I discuss regulatory pathways within the transcription machinery, which involve fuzzy complexes, via protein-protein interactions, post-translational modifications or alternative splicing.

This talk is part of the Experimental and Computational Aspects of Structural Biology and Applications to Drug Discovery series.

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