6LE1

Structure of RRM2 domain of DND1 protein

Summary for 6LE1

Entry DOI	10.2210/pdb6le1/pdb
Descriptor	Dead end protein homolog 1, GLYCEROL, SULFATE ION, ... (4 entities in total)
Functional Keywords	domain swapped dimerisation, transcription
Biological source	Homo sapiens (Human)
Total number of polymer chains	1
Total formula weight	10899.05
Authors	Kumari, P.,Bhavesh, N.S. (deposition date: 2019-11-23, release date: 2020-12-02, Last modification date: 2024-11-13)
Primary citation	Kumari, P.,Bhavesh, N.S. Human DND1-RRM2 forms a non-canonical domain swapped dimer. Protein Sci., 30:1184-1195, 2021 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.3 Å)

Structure validation