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SUMMARY:Pathogenic vs. Reversible Amyloid & Inhibition of Aggregation - Pr
 of David Eisenberg\, Howard Hughes Medical Institute\, UCLA-DOE Institute\
 , Departments of Biological Chemistry and Chemistry & Biochemistry\, UCLA\
 , Los Angeles\, California\, USA
DTSTART:20170301T110000Z
DTEND:20170301T120000Z
UID:TALK71365@talks.cam.ac.uk
CONTACT:Priyanka Joshi
DESCRIPTION:Control of metabolism by compartments is a characteristic of h
 igher cells.  Recent studies have focused on such dynamic intracellular bo
 dies\, inclusions such as stress granules\, P-bodies\, nucleoli\, and meta
 bolic puncta.  These bodies appear as separate phases\, some containing re
 versible\, amyloid-like fibrils formed by interactions of low-complexity p
 rotein domains. We have determined four atomic structures of segments of l
 ow-complexity domains from inclusion-forming proteins\, one determined to 
 1.1 Å resolution by micro-electron diffraction.   These interacting prote
 in segments show common characteristics\, all in contrast to pathogenic am
 yloid: kinked peptide backbones\, smaller surface areas of interaction\, a
 nd domination by interacting aromatic side-chains.  By threading the human
  proteome on our four kinked structures\, we identified more than 1000 low
  complexity domains potentially capable of forming such reversible interac
 tions.  These segments lie in proteins as diverse as RNA binders\, nuclear
  pore proteins\, keratins\, and cornified envelope proteins\, consistent w
 ith the capacity of cells to form a wide variety of dynamic intracellular 
 bodies.  \nIn recent work on pathogenic amyloid\, we have designed inhibit
 ors of aggregation based on atomic structures of segments that drive aggre
 gation.\n              \n
LOCATION:Department of Chemistry\, Cambridge\, Pfizer lecture theatre
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