Related Experiment Videos
Retrovirus envelope domain at 1.7 angstrom resolution
D Fass1, S C Harrison, P S Kim
1Howard Hughes Medical Institute, Cambridge, Massachusetts, 02142, USA.
Nature Structural Biology
|May 1, 1996
Summary
We determined the crystal structure of a Moloney murine leukemia virus (MoMuLV) envelope protein segment. This reveals a trimeric coiled coil structure, offering insights into retroviral fusion proteins and conserved residues.
Area of Science:
- Structural biology
- Virology
- Biochemistry
Background:
- Retrovirus envelope proteins mediate viral entry.
- Understanding their structure is crucial for developing antiviral strategies.
- The Moloney murine leukemia virus (MoMuLV) transmembrane (TM) subunit plays a key role in fusion.
Purpose of the Study:
- To determine the high-resolution crystal structure of an extraviral segment of the MoMuLV TM subunit.
- To provide insights into the structural organization of retroviral surface proteins.
- To establish a model for viral fusion proteins.
Main Methods:
- X-ray crystallography was used to determine the protein structure.
- Comparative analysis with influenza hemagglutinin structures was performed.
Main Results:
- The structure revealed a trimeric coiled coil.
- A hydrophobic cluster was identified at the base of the coiled coil.
- An antiparallel strand packing against the coiled coil was observed.
- Key residues were found to be conserved among various retroviruses and ebola virus.
Conclusions:
- The determined structure provides the first high-resolution view of a retroviral surface.
- This structure serves as a model for a broad class of viral fusion proteins.
- Conserved residues suggest common mechanisms in viral fusion across different virus families.