Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The RIG-I-like receptor LGP2 recognizes the termini of double-stranded RNA.

The Journal of biological chemistry - 15 May 2009

Li Xiaojun, Ranjith-Kumar C T, Brooks Monica T, Dharmaiah S, Herr Andrew B, Kao Cheng, Li Pingwei

Abstract excerpt

The RIG-I-like receptors (RLRs), RIG-I and MDA5, recognize single-stranded RNA with 5' triphosphates and double-stranded RNA (dsRNA) to initiate innate antiviral immune responses. LGP2, a homolog of RIG-I and MDA5 that lacks signaling capability, regulates the signaling of the RLRs. To establish the structural basis of dsRNA recognition by the RLRs, we have determined the 2.0-A resolution crystal structure of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Crystallography, X-Ray
Share to DEAD-box RNA Helicases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Interferon-Induced Helicase, IFIH1

Share to Protein Structure, Tertiary

Share to Receptors, Retinoic Acid

Share to RNA, Double-Stranded

Share to RNA Helicases

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 19278996
DOI: 10.1074/jbc.M900818200
PMCID: PMC2679488

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The RIG-I-like receptor LGP2 recognizes the termini of double-stranded RNA.PMID 19278996Read ↗

Structure and Function of LGP2, a DEX(D/H) Helicase That Regulates the Innate Immunity ResponseSemantic proximity Read ↗

Toward a crystal-clear view of the viral RNA sensing and response by RIG-I-like receptorsSemantic proximity Read ↗

Shared and Unique Functions of the DExD/H-Box Helicases RIG-I, MDA5, and LGP2 in Antiviral Innate ImmunitySemantic proximity Read ↗

Effect of variants in LGP2 on MDA5-mediated activation of interferon response and suppression of hepatitis D virus replicationSemantic proximity Read ↗

Analysis of Porcine RIG-I Like Receptors Revealed the Positive Regulation of RIG-I and MDA5 by LGP2.Semantic proximity Read ↗

Crystal structure of RIG-I C-terminal domain bound to blunt-ended double-strand RNA without 5' triphosphate.Semantic proximity Read ↗

Riplet Ubiquitin Ligase Regulates Innate Antiviral Immune Responses Via Lysine 63-Linked Polyubiquitination of RIG-I and LGP2 and is Essential for Protection Against SARS-CoV-2Semantic proximity Read ↗

Virus Sensor RIG-I Represses RNA Interference by Interacting with TRBP through LGP2 in Mammalian CellsSemantic proximity Read ↗

Discrimination of cytosolic self and non-self RNA by RIG-I-like receptorsSemantic proximity Read ↗

Innate immune sensor LGP2 is cleaved by the Leader protease of foot-and-mouth disease virusSemantic proximity Read ↗

The autoinhibitory CARD2-Hel2i Interface of RIG-I governs RNA selectionSemantic proximity Read ↗

A Distinct Role of Riplet-Mediated K63-Linked Polyubiquitination of the RIG-I Repressor Domain in Human Antiviral Innate Immune ResponsesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.