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SUMMARY:Crystal structure of the Drosophila Toll-Spätzle complex reveals 
 neurotrophin-like binding specificity - Monique Gangloff\, Biochemistry
DTSTART:20140528T091500Z
DTEND:20140528T101500Z
UID:TALK52785@talks.cam.ac.uk
CONTACT:23791
DESCRIPTION:Drosophila Toll plays a critical role in both embryonic develo
 pment and innate immunity in response to an endogenous protein ligand call
 ed Spätzle (Spz). Evolutionary-related Toll-like receptors also function 
 in immunity but are activated directly by pathogen-associated molecules su
 ch as bacterial endotoxin. We determined the crystal structure of dimeric 
 Spz bound to a fragment of the Toll ectodomain encompassing the first 13 l
 eucine-rich repeats at a resolution of 2.35-Å. The cystine-knot domains o
 f Spz bind the concave face of the Toll leucine-rich repeat solenoid in a 
 1:1 complex delineated by N-linked glycans. The binding mode is reminiscen
 t of nerve growth factor (NGF) in complex with neurotrophin receptor p75NT
 R. Despite ellipsoidal truncation and anisotropic scaling of the diffracti
 on data that significantly improved electron density maps\, the two apical
  β-wings and Trp loops of Spz could not be resolved raising the question 
 of their implication in the mechanism of negative cooperativity in Toll si
 gnalling.
LOCATION:Biochemistry Seminar Room\, Sanger Building
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