4lxs

Publication Abstract from PubMed

Drosophila Toll receptors are involved in embryonic development and the immune response of adult flies. In both processes, the only known Toll receptor ligand is the human nerve growth factor-like cystine knot protein Spatzle. Here we present the crystal structure of a 1:1 (nonsignaling) complex of the full-length Toll receptor ectodomain (ECD) with the Spatzle cystine knot domain dimer. The ECD is divided into two leucine-rich repeat (LRR) domains, each of which is capped by cysteine-rich domains. Spatzle binds to the concave surface of the membrane-distal LRR domain, in contrast to the flanking ligand interactions observed for mammalian Toll-like receptors, with asymmetric contributions from each Spatzle protomer. The structure allows rationalization of existing genetic and biochemical data and provides a framework for targeting the immune systems of insects of economic importance, as well as a variety of invertebrate disease vectors.

Structure of the Toll-Spatzle complex, a molecular hub in Drosophila development and innate immunity.,Parthier C, Stelter M, Ursel C, Fandrich U, Lilie H, Breithaupt C, Stubbs MT Proc Natl Acad Sci U S A. 2014 Apr 29;111(17):6281-6. doi:, 10.1073/pnas.1320678111. Epub 2014 Apr 14. PMID:24733933^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.