DNA polymerase template interactions probed by degenerate isosteric nucleobase analogs.
DNA polymerase template interactions probed by degenerate isosteric nucleobase analogs.
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通过简并等排核碱基类似物探测 DNA 聚合酶模板相互作用。
DOI：
10.1016/j.chembiol.2003.08.008
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发表时间：
2003
影响因子：
--
通讯作者：
Davisson,VJo
中科院分区：
文献类型：
--
作者：
Paul,Natasha;Nashine,VishalC;Hoops,Geoffrey;Zhang,Peiming;Zhou,Jie;Bergstrom,DonaldE;Davisson,VJo
The development of novel artificial nucleobases and detailed X-ray crystal structures for primer/template/DNA polymerase complexes provide opportunities to assess DNA-protein interactions that dictate specificity. Recent results have shown that base pair shape recognition in the context of DNA polymerase must be considered a significant component. The isosteric azole carboxamide nucleobases (compounds 1–5; Figure 1) differ only in the number and placement of nitrogen atoms within a common shape and therefore present unique electronic distributions that are shown to dictate the selectivity of template-directed nucleotide incorporation by DNA polymerases. The results demonstrate how nucleoside triphosphate substrate selection by DNA polymerase is a complex phenomenon involving electrostatic interactions in addition to hydrogen bonding and shape recognition. These azole nucleobase analogs offer unique molecular tools for probing nonbonded interactions dictating substrate selection and fidelity of DNA polymerases.
