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The influenza viral genome is composed of eight ribonucleoprotein particles formed by a complex of negative-sense RNA bound to a viral nucleoprotein. Each RNP carries with it an RNA polymerase complex. When the nucleoprotein binds to the viral RNA, it is able to expose the nucleotide bases which allow the viral polymerase to transcribe RNA. At ...
Influenza virus nucleoprotein (NP) is a structural protein which encapsidates the negative strand viral RNA.NP is one of the main determinants of species specificity. The question of how far the NP gene can cross the species barrier by reassortment and become adapted by mutation to the new host has been discussed.
Lyssavirus genomes consist of a negative-sense, single-stranded RNA molecule that encodes five viral proteins: polymerase L, matrix protein M, phosphoprotein P, nucleoprotein N, and glycoprotein G. Genomes are linear, around 11kb in length. [3] Based on recent phylogenetic evidence, lyssaviruses have been categorized into seven major species ...
Nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex (NPC). [1] The nuclear pore complex is a massive structure embedded in the nuclear envelope at sites where the inner and outer nuclear membranes fuse, forming a gateway that regulates the flow of macromolecules between the cell nucleus and the cytoplasm.
Pages for logged out editors learn more. Contributions; Talk; Nucleoproteins
The nucleocapsid (N) protein is a protein that packages the positive-sense RNA genome of coronaviruses to form ribonucleoprotein structures enclosed within the viral capsid. [2] [3] The N protein is the most highly expressed of the four major coronavirus structural proteins. [2]
Heterogeneous nuclear ribonucleoproteins (hnRNPs) are complexes of RNA and protein present in the cell nucleus during gene transcription and subsequent post-transcriptional modification of the newly synthesized RNA (pre-mRNA).
RBPs interact with RNA through various structural motifs. Aromatic amino acid residues in RNA-binding proteins result in stacking interactions with RNA. Lysine residues in the helical portion of RNA binding proteins help to stabilize interactions with other nucleic acids as a result of the force of attraction between the positively-charged lysine side chains and the negatively-charged ...