Grahn E, Stonehouse N J, Murray J B, van den Worm S, Valegård K, Fridborg K, Stockley P G, Liljas L
Department of Molecular Biology, Uppsala University, Sweden.
RNA. 1999 Jan;5(1):131-8. doi: 10.1017/s1355838299981645.
The coat protein of bacteriophage MS2 is known to bind specifically to an RNA hairpin formed within the MS2 genome. Structurally this hairpin is built up by an RNA double helix interrupted by one unpaired nucleotide and closed by a four-nucleotide loop. We have performed crystallographic studies of complexes between MS2 coat protein capsids and four RNA hairpin variants in order to evaluate the minimal requirements for tight binding to the coat protein and to obtain more information about the three-dimensional structure of these hairpins. An RNA fragment including the four loop nucleotides and a two-base-pair stem but without the unpaired nucleotide is sufficient for binding to the coat protein shell under the conditions used in this study. In contrast, an RNA fragment containing a stem with the unpaired nucleotide but missing the loop nucleotides does not bind to the protein shell.
已知噬菌体MS2的外壳蛋白能特异性结合在MS2基因组内形成的一个RNA发夹结构。从结构上看，这个发夹由一个RNA双螺旋构成，该双螺旋被一个未配对的核苷酸打断，并由一个四核苷酸环封闭。我们对MS2外壳蛋白衣壳与四种RNA发夹变体之间的复合物进行了晶体学研究，以评估与外壳蛋白紧密结合的最低要求，并获取有关这些发夹三维结构的更多信息。在本研究使用的条件下，一个包含四个环核苷酸和一个两碱基对茎但没有未配对核苷酸的RNA片段就足以与外壳蛋白壳结合。相比之下，一个包含带有未配对核苷酸的茎但缺少环核苷酸的RNA片段则不会与蛋白壳结合。
