Structural differences between a ras oncogene protein and the normal protein

Structural differences between a ras oncogene protein and the normal protein
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ras癌基因蛋白与正常蛋白之间的结构差异

DOI:
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发表时间:
1989
期刊:
影响因子:
64.8
通讯作者:
Sung
Sung
中科院分区:
综合性期刊1区
文献类型:
--
作者:
L. Tong;A. D. Vos;M. Milburn;J. Jancarik;S. Noguchi;S. Nishimura;K. Miura;E. Ohtsuka;Sung

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One of the most commonly found transforming ras oncogenes in human tumours has a valine codon replacing the glycine codon at position 12 of the normal c-Ha-ras gene1–4. To understand the structural reasons behind cell transformation arising from this single amino acid substitution, we have determined the crystal structure of the GDP-bound form of the mutant protein, p21(Val-12), encoded by this oncogene. We report here the overall structure of p21(Val-12) at 2.2 Å resolution and compare it with the structure of the normal c-Ha-ras protein5. One of the major differences is that the loop of the transforming ras protein that binds the β-phosphate of the guanine nucleotide is enlarged. Such a change in the "catalytic site' conformation could explain the reduced GTPase activity of the mutant6–8, which keeps the protein in the GTP bound 'signal on9 state for a prolonged period of time, ultimately causing cell transformation.
人类 c-H-ras 癌基因产物的结晶。
DOI: 10.1016/0022-2836(88)90345-2
发表时间: 1988
影响因子: 5.6
作者:
Jancarik,J;deVos,A;Kim,SH;Miura,K;Ohtsuka,E;Noguchi,S;Nishimura,S
通讯作者: Nishimura,S
DOI: 10.1126/science.2448879
发表时间: 1988-02-19
期刊: SCIENCE
影响因子: 56.9
作者:
DEVOS, AM;TONG, L;KIM, SH
通讯作者: KIM, SH