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SUMMARY:A structural approach to polyglutamine diseases - Laura Masino
DTSTART:20080213T103000Z
DTEND:20080213T113000Z
UID:TALK10509@talks.cam.ac.uk
CONTACT:Giorgio Favrin
DESCRIPTION:Expansion of unstable CAG trinucleotide repeats coding for pol
 yglutamine is the cause of at least nine inherited neurodegenerative disor
 ders\, that include Huntington’s disease\, Machado–Joseph disease and 
 several other spinocerebellar ataxias. Although the disease mechanisms hav
 e not yet been fully elucidated\, protein misfolding and aggregation seem 
 to be critical steps in disease initiation. Structural information on poly
 glutamine and on the causative proteins is therefore an essential prerequi
 site for understanding pathogenesis and designing effective therapeutic st
 rategies. \nUsing a wide range of biophysical techniques\, we have investi
 gated the structural properties of proteins carrying polyglutamine stretch
 es\, their domain architecture\, stability\, aggregation properties\, and 
 modes of interaction with partners. Our work on a polyglutamine model syst
 em and on the protein ataxin-3\, that causes Machado–Joseph disease\, re
 presents the first structural characterisation of polyglutamine within a p
 rotein context and has highlighted the role of flanking domains in modulat
 ing aggregation\, thereby providing further insights into the mechanisms o
 f neurodegeneration.
LOCATION:Unilever Lecture Theatre\, Unilever Centre\, Department of Chemis
 try
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