5JBG

Crystal structure of chicken LGP2 with 5'ppp 26-mer hairpin RNA with 3' GG overhang and ADP-AlF4-Mg2+ at 2.0 A resolution.

5JBG の概要

• エントリーDOI: 10.2210/pdb5jbg/pdb
• 分子名称: LGP2, RNA (5'-R(*GPPP*GP*AP*GP*CP*GP*UP*GP*CP*CP*GP*GP*GP*CP*AP*CP*GP*CP*UP*CP*CP*GP*G)-3'), ZINC ION, ... (8 entities in total)
• 機能のキーワード: innate immune pattern recognition receptor, rig-i like helicase, dsrna dependent atpase, zinc-containing ctd domain, immune system
• 由来する生物種: Gallus gallus (Chicken); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87124.22

構造登録者

Cusack, S.,Uchikawa, E. (登録日: 2016-04-13, 公開日: 2016-06-01, 最終更新日: 2024-01-10)

主引用文献

Uchikawa, E.,Lethier, M.,Malet, H.,Brunel, J.,Gerlier, D.,Cusack, S.
Structural Analysis of dsRNA Binding to Anti-viral Pattern Recognition Receptors LGP2 and MDA5.
Mol.Cell, 62:586-602, 2016

PubMed Abstract: RIG-I and MDA5 sense virus-derived short 5'ppp blunt-ended or long dsRNA, respectively, causing interferon production. Non-signaling LGP2 appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. Co-crystal structures of chicken (ch) LGP2 with dsRNA display a fully or semi-closed conformation depending on the presence or absence of nucleotide. LGP2 caps blunt, 3' or 5' overhang dsRNA ends with 1 bp longer overall footprint than RIG-I. Structures of 1:1 and 2:1 complexes of chMDA5 with short dsRNA reveal head-to-head packing rather than the polar head-to-tail orientation described for long filaments. chLGP2 and chMDA5 make filaments with a similar axial repeat, although less co-operatively for chLGP2. Overall, LGP2 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. Functionally, RNA binding is required for LGP2-mediated enhancement of MDA5 activation. We propose that LGP2 end-binding may promote nucleation of MDA5 oligomerization on dsRNA.

PubMed: 27203181
DOI: 10.1016/j.molcel.2016.04.021

実験手法

X-RAY DIFFRACTION (2 Å)