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Structural correlates for enhanced stability in the E2 DNA-binding domain from bovine papillomavirus
S Veeraraghavan1, C C Mello, E J Androphy
1Department of Biochemistry, Tufts University School of Medicine, Boston, MA 02111, USA.
Biochemistry
|December 10, 1999
Summary
The bovine papillomavirus E2 protein
Area of Science:
- Structural biology
- Molecular virology
- Biochemistry
Background:
- Papillomaviral E2 proteins are crucial for viral DNA replication and transcriptional regulation.
- Understanding the structure of these proteins is key to deciphering their function.
Purpose of the Study:
- To determine the solution structure of the DNA-binding domain of the bovine papillomavirus type 1 (BPV-1) E2 protein.
- To investigate the role of N-terminal residues in the stability and DNA-binding of the BPV-1 E2 protein.
Main Methods:
- Nuclear magnetic resonance (NMR) spectroscopy (homonuclear and heteronuclear multidimensional).
- Structure calculation using distance and dihedral angle restraints.
- Stability assays comparing different protein constructs.
Main Results:
- The solution structure of the BPV-1 E2 DNA-binding domain homodimer was determined.
- A 16-residue N-terminal extension forms a flap, covering a cavity at the dimer interface and influencing DNA binding.
- The longer protein construct (101 residues) is more stable than the minimal domain (85 residues) due to interactions involving the N-terminal extension.
Conclusions:
- The N-terminal extension of BPV-1 E2 plays a significant role in stabilizing the protein and in DNA binding.
- Structural insights into BPV-1 E2 provide a basis for understanding papillomavirus replication and transcriptional control.
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