Vesiculovirus matrix proteins

Source: Wikipedia, the free encyclopedia.
Vesiculo_matrix
SCOP2
1lg7 / SCOPe / SUPFAM
OPM superfamily381
OPM protein1lg7
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The family of vesiculovirus matrix proteins consists of several

activation of apoptotic pathways causes the inhibition of host gene expression and cell rounding by M protein.[1]

Function

These proteins play a major role in assembly and budding of VSIV virions.

mRNA nuclear export through direct interaction with the host RAE1-NUP98 complex. This inhibits interferon signaling and thus establishment of antiviral state in virus infected cells. In turn, this induces cell-rounding, cytoskeleton disorganization and apoptosis in infected cell. Enveloped viruses acquire their membrane by budding at a membrane of their host cell.[3]

Structure

The structure of these matrix proteins has revealed a single-globular domain with a new fold. The N-terminal part consists of a large five-stranded anti-parallel

C-terminal
part comprises a small two stranded anti-parallel beta-sheet and an alpha-helix.

References

This article incorporates text from the public domain Pfam and InterPro: IPR009397