Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment

被引:237
作者
Vidovic, I
Nottrott, S
Hartmuth, K
Lührmann, R
Ficner, R
机构
[1] Univ Marburg, Inst Mol Biol & Tumorforsch, D-35037 Marburg, Germany
[2] Max Planck Inst Biophys Chem, Abt Zell Biochem, D-37077 Gottingen, Germany
关键词
D O I
10.1016/S1097-2765(00)00131-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We have determined the crystal structure of a spliceosomal RNP complex comprising the 15.5kD protein of the human U4/U6.U5 tri-snRNP and the 5' stem-loop of U4 snRNA. The protein interacts almost exclusively with a purine-rich (5+2) internal loop within the 5' stem-loop, giving an unusual RNA fold characterized by two tandem sheared G-A base pairs, a high degree of purine stacking, and the accommodation of a single RNA base, rotated out of the RNA chain, in a pocket of the protein. Apart from yielding the structure of an important entity in the pre-mRNA splicing apparatus, this work also implies a model for the complex of the 15.5kD protein with box C/D snoRNAs. It additionally suggests a general recognition principle in a novel family of RNA binding proteins.
引用
收藏
页码:1331 / 1342
页数:12
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