| Project/Area Number |
03671024
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Physical pharmacy
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| Research Institution | University of Tokyo |
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Principal Investigator |
SHIMADA Ichio University of Tokyo, Fac.Pharm.Scie., Associate Professor, 薬学部, 助教授 (70196476)
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| Project Period (FY) |
1991 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1993: ¥200,000 (Direct Cost: ¥200,000)
Fiscal Year 1992: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1991: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | NMR / Antibodies / Recognition / Dynamics / Fv / 抗原認識 / タンパク-タンパク相互作用 / 動的立体構造 / タンパク・タンパク相互作用 / 安定同位体標式 |
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| Research Abstract |
An isotope-edited nuclear magnetic resonance study is reported of the Fv fragment, which is the smallest antigen recognition unit composed of V_H and V_L domains. The Fv fragment has been obtained by clostripain digestion of a short-chain anti-dansyl mouse IgG2a monoclonal antibody. A variety of stable-isotope labeled anti-dansyl Fv analogues have been prepared. On the basis of stable isotope-aided heteronuclear and homonuclear two-dimensional NMR spectra, it has been concluded that 1) the dansylring is bound through Tyr-96H and Tyr-104H to both ends of H3 loop, the third hypervariable region of the heavy chain, 2) in the absence of DNS-Lys, the H3 loop displays a significant degree of internal motion and 3) binding of DNS-Lys induces a significant change in the dynamical structure of the H3 loop.
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