| Project/Area Number |
01490007
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
広領域
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| Research Institution | University of Tokyo |
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Principal Investigator |
NAGANO Kozo Univ. Tokyo, Fac. Pharm. Sci., Assoc. Prof., 薬学部, 助教授 (30012636)
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| Co-Investigator(Kenkyū-buntansha) |
ITAI Akiko Univ. Tokyo, Fac. Pharm. Sci., Assoc. Prof., 薬学部, 助教授 (60012647)
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| Project Period (FY) |
1989 – 1990
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| Project Status |
Completed (Fiscal Year 1990)
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| Budget Amount *help |
¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1990: ¥600,000 (Direct Cost: ¥600,000)
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| Keywords | HBcAg dimer / HBsAg inner dimer / HBsAg outer dimer / inter-subunit disulphide bond / packing arrangement / aspaagine-linked sugar chain / sandwiched lipid / MARUZEN model / 表面抗原 / preーS1領域 / preーS2領域 / コア抗原 / HBcAg dimer / HBsAg inner dimer / HBsAG outer dimer / B型肝炎ウィルス / ユア抗原 / アミノ酸配列 / 三次元構造予測 / 2分子会合体 / 小型球形粒子 / Dane粒子 |
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| Research Abstract |
Since it was found that HBcAg has a sequence homology with the capsid protein of rhinovirus, we have built a tertiary structural model of HBcAg based on the beta-barrel structure of human rhinovirus capsid protein obtained from the Protein Data Bank. It was dimerized by two inter-subunit disulphide bonds assigned by a sequence comparison between the HBcAg proteins of human, woodchuck, ground suyirrel and duck. The C-terminal region is a protamine-like sequence. It was built as an alpha-helix by use of MARUZEN model, and the refined coordinates were attached to the C-terminus of the beta-barre structure. When the dimers were arranged that so they satisfied the symmetry of 5-fold and pseudo 6-fold axes, the diameter of the packed model reached nm. It seems most reasonable to assume that HBaAg inner dimers of 180 subunits are packed with their hydrophilic outside inward on the HBcAg core and their hydrophobic beta-sheet upward facing to the hydrophobic beta-sheet of the HBsAg outer dimers of 180 subunits with their hydrophilic surface outside. The diameter of such a packing arrangement of the large particle reaches 42 nm. According to the quantitative analyses of Satoh et al. (1990) about the contents of HBsAg protein and lipids and of Hanaoka et al. (1986) about the composition of asparagine-linked sugar chains of HBsAg, it can be concluded that a small spherical particle of 23 nm in diameter is also composed of inner dimer of 60 subunits with the beta-sheet facing to the beta-sheet of the outer dimer of 60 subunits and that each molecule of HBsAg contain one sugar chain and ll molecules of lipids.
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