CRYSTAL-STRUCTURE AT 1.92 ANGSTROM RESOLUTION OF THE RNA-BINDING DOMAIN OF THE U1A SPLICEOSOMAL PROTEIN COMPLEXED WITH AN RNA HAIRPIN
CRYSTAL-STRUCTURE AT 1.92 ANGSTROM RESOLUTION OF THE RNA-BINDING DOMAIN OF THE U1A SPLICEOSOMAL PROTEIN COMPLEXED WITH AN RNA HAIRPIN
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DOI：
10.1038/372432a0
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发表时间：
1994-12-01
期刊：
影响因子：
64.8
通讯作者：
NAGAI, K
中科院分区：
文献类型：
--
作者：
OUBRIDGE, C;ITO, N;NAGAI, K
以1.92埃的分辨率测定了与21个核苷酸RNA发夹结合的小核核糖核蛋白U1A的RNA结合域的晶体结构。10个核苷酸的RNA环以开放结构与β -sheet表面结合，该环的AUUGCAC序列与保守的RNP1和RNP2基序以及RNP结构域的c端延伸广泛相互作用。这些相互作用包括RNA碱基与芳香蛋白侧链的堆叠，以及许多直接和水介导的氢键。该结构揭示了RNP结构域对序列特异性RNA识别的立体化学基础。
The crystal structure of the RNA-binding domain of the small nuclear ribonucleoprotein U1A bound to a 21-nucleotide RNA hairpin has been determined at 1.92 Angstrom resolution. The ten-nucleotide RNA loop binds to the surface of the beta-sheet as an open structure, and the AUUGCAC sequence of the loop interacts extensively with the conserved RNP1 and RNP2 motifs and the C-terminal extension of the RNP domain. These interactions include stacking of RNA bases with aromatic side chains of proteins and many direct and water-mediated hydrogen bonds. The structure reveals the stereochemical basis for sequence-specific RNA recognition by the RNP domain.