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Journal of Virology, March 2004, p. 3145-3148, Vol. 78, No. 6
0022-538X/04/$08.00+0 DOI: 10.1128/JVI.78.6.3145-3148.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Laboratory of Virology, National Agricultural Research Center, Tsukuba, Ibaraki 305-8666,1 Institute for Protein Research, Osaka University, Suita, Osaka 565-0871,2 Division of Bio-Crystallography Technology, RIKEN Harima Institute, Sayo-gun, Hyogo 679-5148,3 National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8602, Japan,5 Department of Biosciences at Novum, Karolinska Institute, 14157 Huddinge, Sweden4
Received 26 August 2003/ Accepted 21 November 2003
The core protein P3 of Rice dwarf virus constructs asymmetric dimers, one of which is inserted by the amino-terminal region of another P3 protein. The P3 proteins with serial amino-terminal deletions, expressed in a baculovirus system, formed particles with gradually decreasing stability. The capacity for self-assembly disappeared when 52 of the amino-terminal amino acids had been deleted. These results demonstrated that insertion of the amino-terminal arm of one P3 protein into another appears to play an important role in stabilizing the core particles.
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