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SUMMARY:Structure of TRP channel by single particle cryo-EM - Yifan Cheng
DTSTART:20160316T110000Z
DTEND:20160316T120000Z
UID:TALK62581@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:The Transient Receptor Potential (TRP) ion channel is a large 
 and functionally diverse superfamily\, second only to the potassium channe
 ls. Members of TRP channel superfamily include the capsaicin receptor\, TR
 PV1\, and the “wasabi” receptor\, TRPA1. TRPV1 is a polymodal signal d
 etector that resides on primary afferent sensory neurons. It is a heat-act
 ivated cation channel that is also modulated by various inflammatory agent
 s and contributes to acute and persistent pain. TRPA1 activation is trigge
 red by various pungent agonists such as allyl-isothiocyanate from mustard 
 and allicin from garlic\, both generating pungent taste. Enabled by recent
  technological breakthroughs in single particle cryo-EM\, we determined th
 e atomic structures of both TRPV1 and TRPA1. We also utilized their rich p
 harmacological information for structural investigation of these two chann
 els in various functional states\, aiming to elucidate the mechanism of ch
 annel activations.
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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