 |
PDBsum entry 3oja
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Protein binding
|
PDB id
|
|
|
|
3oja
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
A heterodimeric complex of the lrr proteins lrim1 and apl1c regulates complement-Like immunity in anopheles gambiae.
|
|
|
Authors
|
|
R.H.Baxter,
S.Steinert,
Y.Chelliah,
G.Volohonsky,
E.A.Levashina,
J.Deisenhofer.
|
|
|
Ref.
|
|
Proc Natl Acad Sci U S A, 2010,
107,
16817-16822.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
