4XGO

Crystal structure of leucine-rich repeat domain of APL1B

4XGO の概要

• エントリーDOI: 10.2210/pdb4xgo/pdb
• 分子名称: 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)
• 機能のキーワード: protein binding
• 由来する生物種: Anopheles gambiae (African malaria mosquito)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84085.81

構造登録者

Williams, M.,Summers, B.,Baxter, R.H.G. (登録日: 2015-01-01, 公開日: 2015-04-01, 最終更新日: 2024-10-16)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.74 Å)