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Protein found in humans

CD155

CD155
All data from the card 15
Aliases
PVR, CD155, HVED, NECL5, Necl-5, PVS, TAGE4, poliovirus receptor, PVR cell adhesion molecule
External IDs
OMIM: 173850; GeneCards: PVR
PDB
Human UniProt search: PDBe RCSB
Chr.
Chromosome 19 (human)
Band
19q13.31
End
44,666,162 bp
BioGPS
n/a
Databases
NCBI: entry; OMA: entry
Species
Human
Entrez
5817
Ensembl
ENSG00000073008
UniProt
P15151
RefSeq (mRNA)
NM_001135768NM_001135769NM_001135770NM_006505
RefSeq (protein)
NP_001129240NP_001129241NP_001129242NP_006496
Location (UCSC)
Chr 19: 44.64 – 44.67 Mb

CD155 (cluster of differentiation 155), also known as the poliovirus receptor, is a protein that in humans is encoded by the PVR gene. It is a transmembrane protein that is involved in forming junctions between neighboring cells. It is also the molecule that poliovirus uses to enter cells. The gene is specific to the primates.

Function

CD155 is a Type I transmembrane glycoprotein in the immunoglobulin superfamily. Its normal cellular function is in the establishment of intercellular adherens junctions between epithelial cells.

The external domain mediates cell attachment to the extracellular matrix molecule vitronectin, while its intracellular domain interacts with the dynein light chain Tctex-1/DYNLT1.

The role of CD155 in the immune system is unclear, though it may be involved in intestinal humoral immune responses. Subsequent data has also suggested that CD155 may also be used to positively select MHC-independent T cells in the thymus.

Polio

Commonly known as Poliovirus Receptor (PVR), the protein serves as a cellular receptor for poliovirus in the first step of poliovirus replication. Transgenic mice that express the PVR gene have been constructed in order to study polio experimentally.

Structure

CD155 is a transmembrane protein with 3 extracellular immunoglobulin-like domains, D1-D3, where D1 is recognized by the virus.

Low resolution structures of CD155 complexed with poliovirus have been obtained using electron microscopy while a high resolution structures of the ectodomain D1 and D2 of CD155 were solved by x-ray crystallography.

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Text from Wikipedia, CC BY-SA 4.0 · Source article