Getting knotted: a model for the structure and activation of Spätzle.
Sequence analyses show that Spätzle, the Drosophila melanogaster Toll-receptor ligand, shows striking similarity to nerve growth factor and coagulogen. Comparative modelling suggests that Spätzle adopts a cystine-knot fold and forms a dimer that contains a single, intermolecular disulphide bridge. Proteolytically cleaved Spätzle could therefore dimerize and activate the Toll receptor by inducing receptor dimerization.
Dept of Biochemistry, University of Cambridge, UK.
K
K
Mizuguchi
J S
JS
Parker
T L
TL
Blundell
N J
NJ
Gay
D000595:Amino Acid Sequence; D000818:Animals; D001798:Blood Proteins / Q000235:genetics; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000235:genetics / Q000378:metabolism; D019476:Insect Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009414:Nerve Growth Factors / Q000235:genetics; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D001798:Blood Proteins; D029721:Drosophila Proteins; D019476:Insect Proteins; D009414:Nerve Growth Factors; C013445:coagulogen; C086179:spz protein, Drosophila