| 词条 | M1 protein |
| 释义 |
| Symbol = Flu_M1 | Name = Flu_M1 | image = PDB 1ea3 EBI.jpg | width = | caption = influenza virus m1 protein | Pfam = PF00598 | Pfam_clan = | InterPro = IPR001561 | SMART = | PROSITE = | MEROPS = | SCOP = 1aa7 | TCDB = | OPM family = 42 | OPM protein = 1aa7 | CAZy = | CDD = }} The M1 protein is a matrix protein of the influenza virus. It forms a coat inside the viral envelope. This is a bifunctional membrane/RNA-binding protein that mediates the encapsidation of RNA-nucleoprotein cores into the membrane envelope. It is therefore required that M1 binds both membrane and RNA simultaneously.[1] The M1 protein binds to the viral RNA. The binding is not specific to any RNA sequence, and is performed via a peptide sequence rich in basic amino acids. 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 viral ribonucleoproteins from the host cell nucleus, inhibition of viral transcription, and a role in the virus assembly and budding. The protein was found to undergo phosphorylation in the host cell. The M1 protein forms a layer under the patches of host cell membrane that are rich with the viral hemagglutinin, neuraminidase and M2 transmembrane proteins, and facilitates budding of the mature viruses. M1 consists of two domains connected by a linker sequence. The N-terminal domain has a multi-helical structure that can be divided into two subdomains.[2] The C-terminal domain also contains alpha-helical structure. See also
Sources and notes1. ^{{cite journal |vauthors=Sha B, Luo M | title = Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1 | journal = Nat. Struct. Biol. | volume = 4 | issue = 3 | pages = 239–44 |date=March 1997 | pmid = 9164466 | doi = 10.1038/nsb0397-239| url = }} {{Viral proteins}}{{DEFAULTSORT:M1 Protein}}2. ^{{cite journal |vauthors=Arzt S, Baudin F, Barge A, Timmins P, Burmeister WP, Ruigrok RW | title = 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 | journal = Virology | volume = 279 | issue = 2 | pages = 439–46 |date=January 2001 | pmid = 11162800 | doi = 10.1006/viro.2000.0727 | url = }} 4 : Membrane biology|Peripheral membrane proteins|Influenza A virus|Viral structural proteins |
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