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SUMMARY:Serpin metastability and protease inhibition - Dr James Huntington
DTSTART:20080222T115000Z
DTEND:20080222T120000Z
UID:TALK10516@talks.cam.ac.uk
CONTACT:Duncan Simpson
DESCRIPTION:The family of serine protease inhibitors known as the serpins 
 is represented in all branches of life. They have evolved an extraordinary
  mechanism to inhibit proteases that distinguishes them from the 20 other 
 families of serine protease inhibitors\, and renders them uniquely qualifi
 ed to control of the proteolytic pathways essential to life. The mechanism
  resembles the grizzly action of a spring-loaded mousetrap\, where the pro
 tease is the mouse and the serpin is a set and baited trap. When the prote
 ase nibbles the bait\, the trap is sprung\, crushing the unsuspecting prot
 ease. As with a mousetrap\, the active state of a serpin is metastable\, a
 nd the energy released upon conversion to its more stable form is used to 
 crush the protease. By solving crystallographic structures of serpins in v
 arious forms\, we have developed a frame-by-frame cinematic view of this r
 emarkable mechanism.
LOCATION:Sackler Lecture Theatre (Level 7)\, Cambridge Institute for Medic
 al Research
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