Related Experiment Videos
Structure and self-association of the Rous sarcoma virus capsid protein.
R L Kingston1, T Fitzon-Ostendorp, E Z Eisenmesser
1Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Structure (London, England : 1993)
|June 30, 2000
Summary
Rous sarcoma virus (RSV) capsid protein (CA) structures reveal distinct N- and C-terminal domains. In vitro assembly forms ordered tubes and sheets, differing from other retroviruses like HIV-1.
Area of Science:
- Structural biology
- Virology
- Biochemistry
Background:
- Retroviral capsid protein (CA) is crucial for viral structure and function.
- CA forms a shell around genomic RNA in mature retroviruses.
- RSV CA has two independently folded domains.
Purpose of the Study:
- Determine the structures of RSV CA N- and C-terminal domains.
- Investigate the in vitro assembly properties of RSV CA.
- Compare RSV CA assembly with other retroviral CAs.
Main Methods:
- X-ray crystallography for N-terminal domain structure.
- Solution nuclear magnetic resonance (NMR) spectroscopy for C-terminal domain structure.
- Electron microscopy for in vitro assembly analysis.
Main Results:
- RSV CA N-terminal domain has seven alpha helices and a beta hairpin.
- RSV CA C-terminal domain is a four-alpha-helix bundle.
- In vitro, RSV CA assembles into ordered tubes and planar sheets.
Conclusions:
- Tertiary structure of CA is conserved, but sequence variations alter assembly.
- RSV CA exhibits different associative behavior and assembly structures compared to HIV-1 CA.
- CA's tertiary structure conservation contrasts with diverse retroviral core morphologies.