PDBsum entry 3oja

Protein binding

PDB id: 3oja

Contents

Protein chains

482 a.a. *

534 a.a. *

Ligands

NAG-NAG ×4

NAG-NAG-MAN-MAN-MAN-MAN

NAG ×2

Waters ×613

* Residue conservation analysis

PDB id:

3oja

Name:

Protein binding

Title:

Crystal structure of lrim1/apl1c complex

Structure:

Leucine-rich immune molecule 1. Chain: a. Fragment: unp residues 23-509. Engineered: yes. Anopheles plasmodium-responsive leucine-rich repeat protein 1. Chain: b. Fragment: unp residues 140-729. Engineered: yes

Source:

Anopheles gambiae. African malaria mosquito. Organism_taxid: 7165. Strain: g3. Gene: agap006348, lrim1. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Gene: agap007033, apl1c.

Resolution:

2.70Å R-factor: 0.208 R-free: 0.265

Authors:

R.H.G.Baxter,J.Deisenhofer

Key ref:

R.H.Baxter et al. (2010). A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae. Proc Natl Acad Sci U S A, 107, 16817-16822. PubMed id: 20826443

Date:

20-Aug-10 Release date: 22-Sep-10

Protein chain

Q7Q5N3  (Q7Q5N3_ANOGA) -  AGAP006348-PA from Anopheles gambiae

Seq: 509 a.a.

Struc: 482 a.a.

Protein chain

No UniProt id for this chain

Struc: 534 a.a.

Proc Natl Acad Sci U S A 107:16817-16822 (2010)

PubMed id: 20826443

A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae.

R.H.Baxter, S.Steinert, Y.Chelliah, G.Volohonsky, E.A.Levashina, J.Deisenhofer.

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.