6LE1

Structure of RRM2 domain of DND1 protein

6LE1 の概要

• エントリーDOI: 10.2210/pdb6le1/pdb
• 分子名称: Dead end protein homolog 1, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: domain swapped dimerisation, transcription
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10899.05

構造登録者

Kumari, P.,Bhavesh, N.S. (登録日: 2019-11-23, 公開日: 2020-12-02, 最終更新日: 2024-11-13)

主引用文献

Kumari, P.,Bhavesh, N.S.
Human DND1-RRM2 forms a non-canonical domain swapped dimer.
Protein Sci., 30:1184-1195, 2021

PubMed Abstract: 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.

PubMed: 33860980
DOI: 10.1002/pro.4083

実験手法

X-RAY DIFFRACTION (2.3 Å)