Markus M A, Hinck A P, Huang S, Draper D E, Torchia D A
Molecular Structural Biology Unit, National Institute of Dental Research, Bethesda, Maryland 20892-4320, USA.
Nat Struct Biol. 1997 Jan;4(1):70-7. doi: 10.1038/nsb0197-70.
The structure of the C-terminal RNA recognition domain of ribosomal protein L11 has been solved by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. Although the structure can be considered high resolution in the core, 15 residues between helix alpha 1 and strand beta 1 form an extended, unstructured loop. 15N transverse relaxation measurements suggest that the loop is moving on a picosecond-to-nanosecond time scale in the free protein but not in the protein bound to RNA. Chemical shifts differences between the free protein and the bound protein suggest that the loop as well as the C-terminal end of helix alpha 3 are involved in RNA binding.
核糖体蛋白L11 C末端RNA识别结构域的结构已通过异核三维核磁共振光谱法解析。尽管该结构在核心部分可视为高分辨率，但α1螺旋和β1链之间的15个残基形成了一个延伸的无结构环。15N横向弛豫测量表明，该环在游离蛋白中以皮秒到纳秒的时间尺度移动，但在与RNA结合的蛋白中则不然。游离蛋白和结合蛋白之间的化学位移差异表明，该环以及α3螺旋的C末端参与了RNA结合。
