5JB2
Crystal structure of chicken LGP2 with 5'ppp 10-mer dsRNA and ADP-AlF4-Mg2+ at 2.2 A resolution.
Summary for 5JB2
Entry DOI | 10.2210/pdb5jb2/pdb |
Descriptor | LGP2, RNA (5'-R(*GPPP*GP*UP*AP*CP*GP*UP*AP*CP*CP*C)-3'), RNA (5'-R(*GPPP*GP*UP*AP*CP*GP*UP*AP*CP*C)-3'), ... (8 entities in total) |
Functional Keywords | innate immune pattern recognition receptor, rig-i like helicase, dsrna dependent atpase, zinc-containing ctd domain, immune system |
Biological source | Gallus gallus (Chicken) More |
Total number of polymer chains | 3 |
Total formula weight | 85082.19 |
Authors | Cusack, S.,Uchikawa, E. (deposition date: 2016-04-13, release date: 2016-06-01, Last modification date: 2024-01-10) |
Primary citation | 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 Cited by 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: 27203181DOI: 10.1016/j.molcel.2016.04.021 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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