Solution structure of the isolated Pelle death domain.
The interaction between the death domains (DDs) of Tube and the protein kinase Pelle is an important component of the Toll pathway. Published crystallographic data suggests that the Pelle-Tube DD interface is plastic and implies that in addition to the two predominant Pelle-Tube interfaces, a third interaction is possible. We present the NMR solution structure of the isolated death domain of Pelle and a study of the interaction between the DDs of Pelle and Tube. Our data suggests the solution structure of the isolated Pelle DD is similar to that of Pelle DD in complex with Tube. Additionally, they suggest that the plasticity observed in the crystal structure may not be relevant in the functioning death domain complex.
Moncrieffe
Martin C
MC
Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK. mcm35@cam.ac.uk
Stott
Katherine M
KM
Gay
Nicholas J
NJ
D000818:Animals; D018360:Crystallography, X-Ray; D019281:Dimerization; D004330:Drosophila; D029721:Drosophila Proteins / Q000737:chemistry* / Q000502:physiology*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000502:physiology*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D014461:Ultracentrifugation
D029721:Drosophila Proteins; C079896:pll protein, Drosophila; D017346:Protein Serine-Threonine Kinases