Crystal structures of a series of RNA aptamers complexed to the same protein target

被引:93
作者
Rowsell, S
Stonehouse, NJ
Convery, MA
Adams, CJ
Ellington, AD
Hirao, I
Peabody, DS
Stockley, PG
Phillips, SEV [1 ]
机构
[1] Univ Leeds, Sch Biochem & Mol Biol, Leeds LS2 9JT, W Yorkshire, England
[2] Univ Leeds, N England Struct Biol Ctr, Leeds LS2 9JT, W Yorkshire, England
[3] Univ Leeds, Fac Biol Sci, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England
[4] Indiana Univ, Dept Chem, Bloomington, IN 47405 USA
[5] Univ New Mexico, Sch Med, Dept Microbiol & Mol Genet, Albuquerque, NM 87131 USA
[6] Canc Res & Treatment Ctr, Albuquerque, NM 87131 USA
基金
英国惠康基金;
关键词
D O I
10.1038/2946
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 structures, at 2.8 Angstrom resolution, of two different RNA aptamers, each bound to MS2 coat protein. One of the aptamers contains a non-Watson-Crick base pair, while the other is missing one of the unpaired adenines that make sequence-specific contacts in the wild-type complex, Despite these differences, the RNA aptamers bind in the same location on the protein as the wild-type translational operator. Comparison of these new structures with other MS2-RNA complexes allows us to refine further the definition of the minimal recognition elements and suggests a possible application of the MS2 system for routine structure determination of small nucleic acid motifs.
引用
收藏
页码:970 / 975
页数:6
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