Crystal structure of the human nuclear cap binding complex

被引：124

作者：

Mazza, C

Ohno, M

Segref, A

Mattaj, IW

Cusack, S

机构：

[1] European Mol Biol Lab, Grenoble Outstn, F-38042 Grenoble 9, France

[2] European Mol Biol Lab, Gene Express Programme, D-69117 Heidelberg, Germany

来源：

MOLECULAR CELL | 2001年 / 8卷 / 02期

关键词：

D O I：

10.1016/S1097-2765(01)00299-4

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：

The heterodimeric nuclear cap binding complex (CBC) binds to 5'-capped polymerase II transcripts. It enhances the efficiency of several mRNA maturation steps and is essential for U snRNA nuclear export in multicellular eukaryotes. The 2 Angstrom crystal structure of human CBC shows that the large subunit, CBP80, comprises three domains, each containing consecutive helical hairpins and resembling the so-called MIF4G domain found in several other proteins involved in RNA metabolism. The small subunit, CPB20, has an RNP fold and associates with the second and third domains of CBP80. Site-directed mutagenesis revealed 4 residues of CBP20 which are critical for cap binding. A model for cap binding is proposed based on these results and the known mode of binding of RNA to RNP domains.

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收藏

页码：383 / 396

页数：14

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