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首页> 外文期刊>Journal of Molecular Biology >High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor.
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High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor.

机译：异质核糖核蛋白K（c-myc转录因子）C端KH结构域的高精度溶液结构。

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Among it's many reported functions, heterogeneous nuclear ribonucleoprotein (hnRNP) K is a transcription factor for the c- myc gene, a proto-oncogene critical for the regulation of cell growth and differentiation. We have determined the solution structure of the Gly26-->Arg mutant of the C-terminal K-homology (KH) domain of hnRNP K by NMR spectroscopy. This is the first structure investigation of hnRNP K. Backbone residual dipolar couplings, which provide information that is fundamentally different from the standard NOE-derived distance restraints, were employed to improve structure quality. An independent assessment of structure quality was achieved by comparing the backbone15N T1/T2ratios to the calculated structures. The C-terminal KH module of hnRNP K (KH3) is revealed to be a three-stranded beta-sheet stacked against three alpha-helices, two of which are nearly parallel to the strands of the beta-sheet. The Gly26-->Arg mutation abolishes single-stranded DNA binding without altering the overall fold of the protein. This provides a clue to possible nucleotide binding sites of KH3. It appears unlikely that the solvent-exposed side of the beta-sheet will be the site of protein-nucleic acid complex formation. This is in contrast to the earlier theme for protein-RNA complexes incorporating proteins structurally similar to KH3. We propose that the surface of KH3 that interacts with nucleic acid is comparable to the region of DNA interaction for the double-stranded DNA-binding domain of bovine papillomavirus-1 E2 that has a three-dimensional fold similar to that of KH3.
机译：在许多报道的功能中，异质核糖核蛋白（hnRNP）K是c-myc基因的转录因子，c-myc基因是一种原癌基因，对调节细胞的生长和分化至关重要。我们已经通过NMR光谱法确定了hnRNP K的C端K-同源性（KH）域的Gly26-> Arg突变体的溶液结构。这是hnRNP K的首次结构研究。采用了骨干残余偶极偶合来提供与标准NOE衍生的距离限制器根本不同的信息，以提高结构质量。通过将主链15 N T1 / T2比率与计算的结构进行比较，对结构质量进行了独立评估。 hnRNP K（KH3）的C端KH模块显示为三链β-折叠，与三个α-螺旋堆叠，其中两个α-螺旋几乎平行于β-折叠的链。 Gly26-> Arg突变可消除单链DNA结合，而不会改变蛋白质的整体折叠。这为KH3可能的核苷酸结合位点提供了线索。 β-折叠的溶剂暴露面似乎不太可能是蛋白质-核酸复合物形成的部位。这与蛋白质-RNA复合物的早期主题形成了鲜明对比，蛋白质-RNA复合物结合了结构类似于KH3的蛋白质。我们建议，与核酸相互作用的KH3的表面与牛乳头瘤病毒1 E2的双链DNA结合域的DNA相互作用区域可比，该区域具有与KH3相似的三维折叠。

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