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M1 protein

From Wikipedia, the free encyclopedia
Protein family
Flu_M1
influenza virus m1 protein
Identifiers
SymbolFlu_M1
PfamPF00598
InterProIPR001561
SCOP21aa7 /SCOPe /SUPFAM
OPM superfamily42
OPM protein1aa7
Available protein structures:
Pfam  structures /ECOD  
PDBRCSB PDB;PDBe;PDBj
PDBsumstructure summary

TheM1 protein is amatrix protein of theinfluenzavirus. It forms a coat inside theviral envelope. This is a bifunctional membrane/RNA-binding protein that mediates theencapsidation ofnucleoprotein cores into themembrane envelope. It is therefore required that M1binds bothmembrane and RNA simultaneously.[1]

The M1 protein binds to the viralRNA. The binding is not specific to any RNA sequence, and is performed via apeptide sequence rich inbasicamino acids.[citation needed]

It also has multiple regulatory functions, performed by interaction with the components of the host cell. The mechanisms regulated include a role in the export of the viralribonucleoproteins from the hostcell nucleus, inhibition of viraltranscription, and a role in the virus assembly andbudding. The protein was found to undergophosphorylation in the host cell.[citation needed]

The M1 protein forms a layer under the patches of host cell membrane that are rich with the viralhemagglutinin,neuraminidase andM2transmembrane proteins, and facilitatesbudding of the mature viruses.[citation needed]

M1 consists of twodomains connected by a linkersequence. The N-terminaldomain has a multi-helicalstructure that can be divided into two subdomains.[2] The C-terminal domain also containsalpha-helicalstructure.

See also

[edit]

Sources and notes

[edit]
  1. ^Sha B, Luo M (March 1997). "Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1".Nat. Struct. Biol.4 (3):239–44.doi:10.1038/nsb0397-239.PMID 9164466.S2CID 22521750.
  2. ^Arzt S, Baudin F, Barge A, Timmins P, Burmeister WP, Ruigrok RW (January 2001)."Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer".Virology.279 (2):439–46.doi:10.1006/viro.2000.0727.PMID 11162800.
DNA
linear ds-DNA
(Duplodnaviria,
Varidnaviria)
Herpes simplex
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Epstein–Barr
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