Related Experiment Video
Updated: Feb 9, 2026
06:25
Analysis of Simian Immunodeficiency Virus-specific CD8+ T-cells in Rhesus Macaques by Peptide-MHC-I Tetramer Staining
Published on: December 23, 2016
9.6K
West Nile virus core protein; tetramer structure and ribbon formation
Terje Dokland1, Martin Walsh, Jason M Mackenzie
1Institute of Molecular and Cell Biology, Singapore, Republic of Singapore. dokland@uab.edu
Structure (London, England : 1993)
|July 10, 2004
Summary
Researchers determined the crystal structure of the West Nile virus (WNV) core protein. This finding advances understanding of WNV, a significant U.S. health threat, and its internal structure.
Area of Science:
- Structural biology
- Virology
- Molecular biology
Background:
- West Nile virus (WNV) is a significant public health concern in the U.S.
- WNV belongs to the Flaviviridae family, known for causing human diseases.
- The WNV core (C) protein is integral to the virus's structure, associating with its RNA genome.
Purpose of the Study:
- To elucidate the three-dimensional structure of the West Nile virus core (C) protein.
- To provide insights into the molecular organization of the WNV virion.
Main Methods:
- X-ray crystallography was employed to determine the protein structure.
- Analysis of the C protein's quaternary structure and its components.
Main Results:
- The crystal structure of the WNV C protein was determined.
- The C protein comprises four alpha helices.
- The protein forms dimers that further assemble into tetramers.
- These tetramers organize into filamentous ribbons.
Conclusions:
- The determined structure reveals a novel arrangement of alpha helices within the WNV C protein tetramers.
- The filamentous ribbon structure offers insights into the organization of the viral core.
- This structural information may aid in the development of antiviral strategies against WNV.
Related Concept Videos
02:15Protein and Protein Structure
88.4K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
88.4K
02:10The Nucleosome Core Particle
14.6K
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
14.6K
01:56Structural Protein Function
30.0K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
30.0K
01:56Structural Protein Function
3.3K
No description available
3.3K
02:41Protein Complex Assembly
16.8K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.8K
00:56Viral Structure
74.7K
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.
74.7K