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首页> 外文期刊>Journal of Molecular Biology >X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21(H-RAS) COMPLEXED WITH CAGED GTP AND MANT DGPPNHP
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X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21(H-RAS) COMPLEXED WITH CAGED GTP AND MANT DGPPNHP

机译：笼蔽GTP和Mant DGPPNHP的致癌产物P21（H-RAS）的催化范围的X射线晶体结构分析

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The X-ray structures of the 1:1 complexes formed between p21(H-ras) (residues 1 to 166) and the nucleotides P-3-1-(2-nitrophenyl)ethyl guanosine triphosphate (''caged GTP''; pure R- and S-diastereomers) and 3'-O-(N-methylanthraniloyl)-2'-deoxyguanosine 5'-(beta,gamma-imido)-triphosphate (''mant dGppNHp''), have been refined to an R-factor of 21.4% (R-caged GTP, 1.85 Angstrom resolution), 18.9% (S-caged GTP, 2.5 Angstrom resolution) and 17.6% (mant dGppNHp, 2.7 Angstrom resolution), respectively. Details of the structure determination, refinement and the structures themselves are presented. The overall structures of the complexes are identical in terms of the general organization of their secondary structure elements and are also identical to that reported for the analogous complex of p21(H-ras) with GppNHp. The binding of the GTP part is not significantly affected by the additional aromatic group (cage and mant, respectively) in contrast to the original observation on p21:caged GTP using the racemic mixture of R- and S-caged GTP. The main differences in the structures are observed in the region of loop L2 (residues Glu31 to Thr35) where the additional aromatic group attached to the nucleotide comes very close to the side-chain of Tyr32, including backbone displacements of 2.6 Angstrom, 2.2 Angstrom and 0.3 Angstrom for the residues from Glu31 to Thr35 for R-caged, S-caged GTP and mant dGppNHp, respectively. The refined structures provide additional data for the design of new nucleotide analogs and the importance of their stereochemistry as well as for the design of new mutant forms of p21(H-ras) for further biochemical investigations. The binding mode of mant dGppNHp reveals significant features for the understanding of the fluorescence signals observed in solution. (C) 1995 Academic Press Limited [References: 81]
机译：p21（H-ras）（残基1至166）与核苷酸P-3-1-（2-硝基苯基）乙基鸟苷三磷酸（笼中GTP）之间形成的1：1配合物的X射线结构;纯的R和S-非对映异构体）和3'-O-（N-甲基蒽基）-2'-脱氧鸟苷5'-（β，γ-亚氨基）-三磷酸酯（``mant dGppNHp''）已精制为R因子分别为21.4％（R笼式GTP，1.85埃分辨率），18.9％（S笼形GTP，2.5埃分辨率）和17.6％（mand dGppNHp，2.7埃分辨率）。给出了结构确定，改进和结构本身的详细信息。配合物的总体结构在其二级结构元素的一般组织方面是相同的，并且也与报道的p21（H-ras）与GppNHp的相似配合物相同。与使用R和S笼蔽的GTP的外消旋混合物在p21：笼蔽的GTP上的原始观察结果相反，GTP部分的结合不受其他芳香基团（分别为笼和age）的显着影响。在环L2的区域（残基Glu31至Thr35）中观察到了结构上的主要差异，其中与核苷酸连接的其他芳族基团非常接近Tyr32的侧链，包括2.6埃，2.2埃和对于R笼，S笼GTP和mand dGppNHp，Glu31至Thr35的残基分别为0.3埃。精炼的结构为新核苷酸类似物的设计及其立体化学的重要性以及为进一步生化研究设计新的p21（H-ras）突变形式的设计提供了额外的数据。 mant dGppNHp的结合模式揭示了重要的功能，可用于理解溶液中观察到的荧光信号。 （C）1995 Academic Press Limited [参考：81]

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