Imaging

@article{RH2010,

title = {A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae},

author = {Richard H Baxter and Stefanie Steinert and Y Chelliah and Gloria Volohonsky and Elena A Levashina and J Deisenhofer},

url = {http://www.ncbi.nlm.nih.gov/pubmed/20826443},

year  = {2010},

date = {2010-09-08},

volume = {107},

number = {39},

pages = {16817-22},

abstract = {The leucine-rich repeat (LRR) proteins LRIM1 and APL1C control the function of the complement-like protein TEP1 in Anopheles mosquitoes. The molecular structure of LRIM1 and APL1C and the basis of their interaction with TEP1 represent a new type of innate immune complex. The LRIM1/APL1C complex specifically binds and solubilizes a cleaved form of TEP1 without an intact thioester bond. The LRIM1 and APL1C LRR domains have a large radius of curvature, glycosylated concave face, and a novel C-terminal capping motif. The LRIM1/APL1C complex is a heterodimer with a single intermolecular disulfide bond. The structure of the LRIM1/APL1C heterodimer reveals an interface between the two LRR domains and an extensive C-terminal coiled-coil domain. We propose that a cleaved form of TEP1 may act as a convertase for activation of other TEP1 molecules and that the LRIM1/APL1C heterodimer regulates formation of this TEP1 convertase.},

keywords = {APL1C, LRIM1},

pubstate = {published},

tppubtype = {article}

}