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SUMMARY:Fuzzy complexes: ambiguity in protein-protein and protein-DNA inte
 ractions - Professor Monika Fuxreiter Institute of Enzymology\, Budapest\,
  HUNGARY and LMB\, MRC\, Cambridge\, UK
DTSTART:20111116T101500Z
DTEND:20111116T111500Z
UID:TALK34627@talks.cam.ac.uk
CONTACT:23791
DESCRIPTION:For a long time\, protein function was thought to be determine
 d by a well-defined three-dimensional structure. Recently it has been real
 ized however\, that many proteins disobey this classical structure-functio
 n paradigm. Intrinsically disordered (ID) proteins function as multiplicit
 y of structures and their activities can only be described by stochastic s
 tructure-function relationships. In their complex forms however\, ID prote
 ins were thought to loose their plasticity and behave similarly to globula
 r proteins. Although various ID regions indeed fold upon binding\, this vi
 ew is not valid in general. ID segments usually interact with their partne
 rs via short motifs\, which require malleable environments to function. Co
 nsequently\, ID regions could retain their disordered state in the complex
 \, a phenomenon termed as fuzziness. The number of structurally characteri
 zed fuzzy complexes\, both with protein and DNA\, rapidly increases. I des
 cribe 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 conformationa
 l 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-transla
 tional modifications or alternative splicing. 
LOCATION:Perham's seminar room
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