Lymphotoxin beta receptor

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Lymphotoxin beta receptor

Lymphotoxin beta receptor (LTBR), also known as tumor necrosis factor receptor superfamily member 3 (TNFRSF3), is a cell surface receptor for lymphotoxin involved in apoptosis and cytokine release.[5][6][7] It is a member of the tumor necrosis factor receptor superfamily.

Quick Facts LTBR, Available structures ...
LTBR
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Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesLTBR, CD18, D12S370, LT-BETA-R, TNF-R-III, TNFCR, TNFR-RP, TNFR2-RP, TNFR3, TNFRSF3, lymphotoxin beta receptor
External IDsOMIM: 600979; MGI: 104875; HomoloGene: 1753; GeneCards: LTBR; OMA:LTBR - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001270987
NM_002342

NM_010736

RefSeq (protein)

NP_001257916
NP_002333

NP_034866

Location (UCSC)Chr 12: 6.38 – 6.39 MbChr 6: 125.28 – 125.29 Mb
PubMed search[3][4]
Wikidata
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Function

The protein encoded by this gene is a member of the tumor necrosis factor (TNF) family of receptors. It is expressed on the surface of most cell types, including cells of epithelial and myeloid lineages, but not on T and B lymphocytes. The protein specifically binds the lymphotoxin membrane form (a complex of lymphotoxin-alpha and lymphotoxin-beta). The encoded protein and its ligand play a role in the development and organization of lymphoid tissue and transformed cells. Activation of the encoded protein can trigger apoptosis.[5]

Not only does the LTBR help trigger apoptosis, it can lead to the release of the cytokine interleukin 8. Overexpression of LTBR in HEK293 cells increases IL-8 promoter activity and leads to IL-8 release. LTBR is also essential for development and organization of the secondary lymphoid organs and chemokine release.[8]

Structure

The Ramachandran plots show that 64.6% of all residues were in a favored region. This structure was found using X-ray diffraction. The resolution is 3.50 angstroms. The alpha and beta angles are 90 degrees while the gamma angle is 120 degrees.[9]

Interactions

Lymphotoxin beta receptor has been shown to interact with Diablo homolog[10] and TRAF3.[11][12][13]

References

Further reading

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