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SUMMARY:Structural Studies on the Regulation of Protein Kinases: EGFR and 
 CamK-II - John Kuriyan\, HHMI\, University of California\, Berkeley
DTSTART:20111031T161500Z
DTEND:20111031T180000Z
UID:TALK31427@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:In this lecture I will discuss our recent analyses of two prot
 ein kinases. The epidermal growth factor receptor (EGFR) is a receptor tyr
 osine kinase involved in cell growth that is often misregulated in cancer.
  We have elucidated the important role that the juxtamembrane segment and 
 transmembrane helix of the receptor play in stabilizing an activating asym
 metric dimer of the kinase domains\, and I will discuss how these features
  allows specificity in signal transduction. Calcium/calmodulin dependent k
 inase II (CaMKII) forms a highly conserved dodecameric assembly that is se
 nsitive to the frequency of calcium pulse trains. We have determined the c
 rystal structure of an autoinhibited full-length human CaMKII holoenzyme\,
  revealing an unexpected compact arrangement of kinase domains docked agai
 nst a central hub\, with the calmodulin binding site completely inaccessib
 le. Our studies suggest a simple mechanism for tuning the calcium response
  without changes in either the hub or the kinase domains.
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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