Related Experiment Video
Updated: Oct 19, 2025

09:39
Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein
Published on: April 21, 2015
17.9K
New structural insights into the multifunctional influenza A matrix protein 1
Julia Peukes1,2, Xiaoli Xiong1,3, John A G Briggs1,4
1Structural Studies Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
FEBS Letters
|September 21, 2021
Summary
Influenza A virus matrix protein 1 (M1) forms filaments, revealing its structure and function in virus assembly and infection. This provides a molecular basis for understanding M1
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- Influenza A virus matrix protein 1 (M1) is crucial for viral structure and replication.
- M1 protein is the most abundant protein in influenza virions.
- M1 plays key roles in nuclear RNA export, virus assembly, and disassembly.
Purpose of the Study:
- To compare and discuss the first structures of full-length M1.
- To explore the implications of M1 structures for its functions.
- To understand the molecular mechanisms of M1 in virus life cycle.
Main Methods:
- Structural analysis of full-length M1.
- Comparison of two recent M1 structure publications.
- In vitro filament assembly assays.
Main Results:
- First structures of full-length M1 reveal filament assembly via N- and C-terminal domains.
- Assembled M1 filaments resemble the virion endoskeleton.
- Structures offer molecular insights into M1's multifunctional roles.
Conclusions:
- M1 protein structures provide a molecular basis for understanding its functions.
- M1 filament formation is key to virus assembly and M1's role in infection.
- Further research can elucidate M1's interactions with viral ribonucleoproteins.
Related Concept Videos
Leaky Scanning
5.3K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.3K
Protein Complexes with Interchangeable Parts
2.7K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.7K
Matrix Proteoglycans and Glycoproteins
4.2K
Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
4.2K
Viral Structure
67.3K
Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
67.3K

