4XGO
Crystal structure of leucine-rich repeat domain of APL1B
Summary for 4XGO
Entry DOI | 10.2210/pdb4xgo/pdb |
Descriptor | Anopheles 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 Keywords | protein binding |
Biological source | Anopheles gambiae (African malaria mosquito) |
Total number of polymer chains | 2 |
Total formula weight | 84085.81 |
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 citation | Williams, 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: 25775123DOI: 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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