1998 Fiscal Year Final Research Report Summary
The Structure-function Relationships of the Human Immunodeficiency Virus Type-2 (HIV-2) Nucleocapsid protein
| Project/Area Number |
09680656
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Kitasato University |
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Principal Investigator |
MAEDA Tadakazu School of Science, Kitasato University, Professor, 理学部, 教授 (90265728)
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| Co-Investigator(Kenkyū-buntansha) |
KOHNO Toshiyuki Mitsubishi Kasei Institute of Life Science, Senior Researcher, 生命科学研究所, 副主任研究員
KODERA Yoshio School of Science, Kitasato University, lecturer, 理学部, 講師 (60265733)
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| Project Period (FY) |
1997 – 1998
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| Keywords | NMR / three-dimensional structure / nucleocapsid protein / HIV-2 / structure-function relationships / NCp8 |
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| Research Abstract |
Retroviral NC protein is a multi-functional protein essential for RNA genome packaging and infectivity of the viruses. The NC protein, NCp8, of HIV-2 is a 49 amino acid peptide containing two zinc fingers of the type C-X_2-C-X_4-H-X_4-C connected by seven amino acids residues called "basic amino acid cluster". In the present study, the three-dimensional structures of NCp8-derived peptides , NCp8-fl and NCp8-f2, were determined by H NMR spectroscopy with simulated annealing calculations.
1. Three-dimensional structure of NCp8-f1
NCp8-f1 is a 29 amino acid peptide including the N-terminal zinc finger and the basic amino acid cluster. It has been shown that this region of NCp8 is the minimal active domain. From the result of the structural analysis, the RMSD of the 15 converged structures was 0.29 0.04 A for the backbone atoms (N, Calpha, C). Interestingly, the basic amino acid cluster itself was well-defined with a loop-like conformation in which three arginine residues in the cluster and one arginine residue in the zinc finger are located on the same side of the molecule and exposed to the solvent. The structure-function relationships was discussed on the basis of the comparison of this structure with NC proteins of HIV-1 (NCp7) and of Molony murine leukemia virus (NCp10).
2. Three-dimensional structure of NCpS-f2
NCp8-f2 is a 27 amino acid peptide, which includes the C-terminal zinc finger and the basic amino acid cluster. The three-dimensional structure of NCp8-f2 was determined. The backbone atoms of the zinc finger converged well and the structure was similar to that of the second zinc finger of NCp7. The basic amino acid cluster adopt a loop-like conformation. The activity of the RNA recognition of NCpS-f2 is different from that of the corresponding region of NCp7. We discussed the structure-function relationships of NCp8-f2 in comparison with those of NCp7 and NCp8-f1.
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