LGP2

 Probable ATP-dependent RNA helicase DHX58 also known as RIG-I-like receptor 3 (RLR-3) or RIG-I-like receptor LGP2 (RLR) is a RIG-I-like receptor dsRNA helicase enzyme that in humans is encoded by the DHX58 gene.[5][6] The protein encoded by the gene DHX58 is known as LGP2 (Laboratory of Genetics and Physiology 2).[5][7][8]

DHX58
Protein DHX58 PDB 2RQA.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDHX58, D11LGP2, D11lgp2e, LGP2, RLR-3, DEXH-box helicase 58
External IDsOMIM608588 MGI1931560 HomoloGene69371 GeneCardsDHX58
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for DHX58
Genomic location for DHX58
Band17q21.2Start42,101,404 bp[1]
End42,112,714 bp[1]
RNA expression pattern
PBB GE LGP2 219364 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_024119

NM_030150

RefSeq (protein)

NP_077024

NP_084426

Location (UCSC)Chr 17: 42.1 – 42.11 MbChr 11: 100.69 – 100.7 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Structure and functionEdit

LGP2 was first identified and characterized in the context of mammary tissue in 2001,[5] but its function has been found to be more relevant to the field of innate antiviral immunity. LGP2 has been found to be essential for producing effective antiviral responses against many viruses that are recognized by RIG-I and MDA5.[9]

Since LGP2 lacks CARD domains, its effect on downstream antiviral signaling is likely due to interaction with dsRNA viral ligand or the other RLRs (RIG-I and MDA5).[10]

LGP2 has been shown to directly interact[10] with RIG-I through its C-terminal repressor domain (RD). The primary contact sites in this interaction is likely between the RD of LGP2 and the CARD or helicase domain of RIG-I as it is seen with RIG-I self-association,[10] but this has not been confirmed. The helicase activity of LGP2 has been found to be essential for its positive regulation of RIG-I signaling.[9] Overexpression of LGP2 is able to inhibit RIG-I-mediated antiviral signaling both in the presence and absence of viral ligands.[10][11][12] This inhibition of RIG-I signaling is not dependent upon the ability of LGP2 to bind viral ligands and is therefore not due to ligand competition.[7][13] Although LGP2 binds to dsRNA with higher affinity,[12] it is dispensable for RIG-I-mediated recognition of synthetic dsRNA ligands.[9] RIG-I, when overexpressed[7] and in LGP2 knock-down studies,[14] has been shown to induce antiviral response in the absence of viral ligand.

This article uses material from the Wikipedia article
 Metasyntactic variable, which is released under the 
Creative Commons
Attribution-ShareAlike 3.0 Unported License
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