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- 저자 : Shigeyuki Yokoyama ( Jong Myung Ha ) (검색결과 1 건)
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인간의 c - Ha - ras 발암성 단백질에 결합되어 있는 GDP 와 GTPγ의 형태 비교
하종명,Gota Kawai,Tatsuo Miyazawa,Shigeyuki Yokoyama ( Jong Myung Ha ) 생화학분자생물학회 1993 BMB Reports Vol.26 No.1
A normal ras protein and two of the mutant proteins were prepared to investigate the biochemical properties of ras proteins produced by ras genes. The methods for the preparation of ras proteins include 1) the truncation of c-Ha-ras protein at the position 18 from carboxy-terminal producing [ras(G12/1-171) protein], 2) the replacement of glycine by valine at position 12 of the ras protein from amino-terminal followed by the truncation of c-Ha-ras protein at the position 18 from carboxy-terminal [ras(V12/1-171) protein], 3) the replacement of glutamine by leucine at the position 61 followed by the truncation of c-Ha-ras protein at the position 18 from carboxy-terminal [ras(L61/1-171) protein]. The proton resonances of H8(guanine) and H1`, H2`, H3`, H4`, H5` (ribose) of the GDP and the GTP_γS [Guanosine 5`-0-(3-thiotriphosphate)] bound to ras(1-171) proteins were identified. By numerical simulation of these irradiated time-dependent NOE profiles, the conformations of the protein-bound GDP and GTP S were elucidated. The guanosine moieties of GDPs bound to three ras(1-171) proteins take the anti form about the N-glycosidic bond with a dihedral angle of χ= -120° and the ribose ring take the C2`-endo forms that were independent with point mutation. In contrast to the conformation of the bound GDP, the guanosine moieties of GTP_γSs bound to ras(1-171) proteins had anti-C3`-endo form and a dihedral angle of χ=-80°, and were not affected by the point mutation of ras(1-171) protein. The role of the interaction between the bound guanine nucleotide and effector region is discussed with regard to the mechanism of the ras proteins.
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