Nagai K, Oubridge C, Jessen T H, Li J, Evans P R
MRC Laboratory of Molecular Biology, Cambridge, UK.
Nature. 1990 Dec 6;348(6301):515-20. doi: 10.1038/348515a0.
The crystal structure of the RNA binding domain of the U1 small nuclear ribonucleoprotein A, which forms part of the ribonucleoprotein complex involved in the excision of introns, has been solved. It contains a four-stranded beta sheet and two alpha helices. The highly conserved segments designated RNP1 and RNP2 lie side by side on the middle two beta strands. U1 RNA binding studies of mutant proteins suggest that the RNA binds to the four-stranded beta sheet and to the flexible loops on one end.
U1小核核糖核蛋白A的RNA结合结构域的晶体结构已被解析，该蛋白是参与内含子切除的核糖核蛋白复合体的一部分。它包含一个四链β折叠和两个α螺旋。高度保守的RNP1和RNP2片段并排位于中间的两条β链上。对突变蛋白的U1 RNA结合研究表明，RNA与四链β折叠以及一端的柔性环结合。
