Varani G, Nagai K
MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Annu Rev Biophys Biomol Struct. 1998;27:407-45. doi: 10.1146/annurev.biophys.27.1.407.
The ribonucleoprotein (RNP) domain is one of the most common eukaryotic protein folds. Proteins containing RNP domains function in important steps of posttranscriptional regulation of gene expression by directing the assembly of multiprotein complexes on primary transcripts, mature mRNAs, and stable ribonucleoprotein components of the RNA processing machinery. The diverse functions performed by these proteins depend on their dual ability to recognize RNA and to interact with other proteins, often utilizing specialized auxiliary domains. Crystallographic and NMR structures of several RNP domains and a handful of structures of RNA-protein complexes have begun to reveal the molecular basis for RNP-RNA recognition.
核糖核蛋白（RNP）结构域是真核生物中最常见的蛋白质折叠结构之一。含有RNP结构域的蛋白质在基因表达的转录后调控的重要步骤中发挥作用，通过引导多蛋白复合物在初级转录本、成熟mRNA以及RNA加工机制的稳定核糖核蛋白组分上组装。这些蛋白质执行的多种功能取决于它们识别RNA以及与其他蛋白质相互作用的双重能力，通常利用专门的辅助结构域。几种RNP结构域的晶体学和核磁共振结构以及少数RNA-蛋白质复合物的结构已经开始揭示RNP-RNA识别的分子基础。
