Transcription Regulation Group, International Centre for Genetic Engineering and Biotechnology (ICGEB), New Delhi, India.
Protein Sci. 2021 Jun;30(6):1184-1195. doi: 10.1002/pro.4083. Epub 2021 Apr 26.
RNA recognition motif (RRM) being the most abundant RNA binding domain in eukaryotes, is a major player in cellular regulation. Several variations in the canonical βαββαβ topology have been observed. We have determined the 2.3 Å crystal structure of the human DND1-RRM2 domain. The structure revealed an interesting non-canonical RRM fold, which is maintained by the formation of a 3D domain swapped dimer between β and β strands across protomers. We have delineated the structural basis of the stable domain swapped dimer formation using the residue level dynamics of protein explored by NMR spectroscopy and MD simulations. Our structural and dynamics studies substantiate major determinants and molecular basis for domain swapped dimerization observed in the RRM domain.
RNA 识别模体（RRM）是真核生物中最丰富的 RNA 结合域，是细胞调节的主要参与者。已经观察到在典型的 βαββαβ 拓扑结构中有几种变体。我们已经确定了人类 DND1-RRM2 结构域的 2.3Å 晶体结构。该结构揭示了一种有趣的非典型 RRM 折叠，该折叠通过形成跨原体β和β链之间的 3D 结构域交换二聚体来维持。我们使用 NMR 光谱和 MD 模拟探索的蛋白质残基水平动力学来描绘稳定的结构域交换二聚体形成的结构基础。我们的结构和动态研究证实了在 RRM 结构域中观察到的结构域交换二聚化的主要决定因素和分子基础。
