3O6N

Crystal Structure of APL1 leucine-rich repeat domain

Summary for 3O6N

• Entry DOI: 10.2210/pdb3o6n/pdb
• Related: 3O53
• Descriptor: APL1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: leucine-rich repeat, protein binding
• Biological source: Anopheles gambiae (African malaria mosquito)
• Total number of polymer chains: 1
• Total formula weight: 45996.98

Authors

Baxter, R.H.G.,Steinert, S.,Chelliah, Y.,Volohonsky, G.,Levashina, E.A.,Deisenhofer, J. (deposition date: 2010-07-29, release date: 2010-09-22, Last modification date: 2024-10-16)

Primary citation

Baxter, R.H.,Steinert, S.,Chelliah, Y.,Volohonsky, G.,Levashina, E.A.,Deisenhofer, J.
A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae.
Proc.Natl.Acad.Sci.USA, 107:16817-16822, 2010

PubMed 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.

PubMed: 20826443
DOI: 10.1073/pnas.1010575107

Experimental method

X-RAY DIFFRACTION (1.85 Å)