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4XGO

Crystal structure of leucine-rich repeat domain of APL1B

Summary for 4XGO
Entry DOI10.2210/pdb4xgo/pdb
DescriptorAnopheles Plasmodium-responsive Leucine-rich repeat protein 1B, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, PHOSPHATE ION, ... (8 entities in total)
Functional Keywordsprotein binding
Biological sourceAnopheles gambiae (African malaria mosquito)
Total number of polymer chains2
Total formula weight84085.81
Authors
Williams, M.,Summers, B.,Baxter, R.H.G. (deposition date: 2015-01-01, release date: 2015-04-01, Last modification date: 2024-10-16)
Primary citationWilliams, M.,Summers, B.J.,Baxter, R.H.
Biophysical Analysis of Anopheles gambiae Leucine-Rich Repeat Proteins APL1A1, APLB and APL1C and Their Interaction with LRIM1.
Plos One, 10:e0118911-e0118911, 2015
Cited by
PubMed Abstract: Natural infection of Anopheles gambiae by malaria-causing Plasmodium parasites is significantly influenced by the APL1 genetic locus. The locus contains three closely related leucine-rich repeat (LRR) genes, APL1A, APL1B and APL1C. Multiple studies have reported the participation of APL1A-C in the immune response of A. gambiae to invasion by both rodent and human Plasmodium isolates. APL1C forms a heterodimer with the related LRR protein LRIM1 via a C-terminal coiled-coil domain that is also present in APL1A and APL1B. The LRIM1/APL1C heterodimer protects A. gambiae from infection by binding the complement-like protein TEP1 to form a stable and active immune complex. Here we report solution x-ray scatting data for the LRIM1/APL1C heterodimer, the oligomeric state of LRIM1/APL1 LRR domains in solution and the crystal structure of the APL1B LRR domain. The LRIM1/APL1C heterodimeric complex has a flexible and extended structure in solution. In contrast to the APL1A, APL1C and LRIM1 LRR domains, the APL1B LRR domain is a homodimer. The crystal structure of APL1B-LRR shows that the homodimer is formed by an N-terminal helix that complements for the absence of an N-terminal capping motif in APL1B, which is a unique distinction within the LRIM1/APL1 protein family. Full-length APL1A1 and APL1B form a stable complex with LRIM1. These results support a model in which APL1A1, APL1B and APL1C can all form an extended, flexible heterodimer with LRIM1, providing a repertoire of functional innate immune complexes to protect A. gambiae from a diverse array of pathogens.
PubMed: 25775123
DOI: 10.1371/journal.pone.0118911
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.74 Å)
Structure validation

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