6JVX

Crystal structure of RBM38 in complex with RNA

Summary for 6JVX

• Entry DOI: 10.2210/pdb6jvx/pdb
• Descriptor: RNA-binding protein 38, RNA (5'-R(*UP*GP*UP*GP*UP*GP*UP*GP*UP*GP*UP*G)-3'), SULFATE ION, ... (4 entities in total)
• Functional Keywords: rbm38, rna binding, translational regulation, rna binding protein, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 17908.94

Authors

Qian, K.,Li, M.,Wang, J.,Zhang, M.,Wang, M. (deposition date: 2019-04-17, release date: 2020-01-01, Last modification date: 2023-11-22)

Primary citation

Qian, K.,Li, M.,Wang, J.,Zhang, M.,Wang, M.
Structural basis for mRNA recognition by human RBM38.
Biochem.J., 477:161-172, 2020

PubMed Abstract: RNA-binding protein RBM38 was reported to bind the mRNA of several p53-related genes through its RRM domain and to up-regulate or down-regulate protein translation by increasing mRNA stability or recruitment of other effector proteins. The recognition mechanism, however, for RNA-binding of RBM38 remains unclear. Here, we report the crystal structure of the RRM domain of human RBM38 in complex with a single-stranded RNA. Our structural and biological results revealed that RBM38 recognizes G(U/C/A)GUG sequence single-stranded RNA in a sequence-specific and structure-specific manner. Two phenylalanine stacked with bases of RNA were crucial for RNA binding, and a series of hydrogen bonds between the base atoms of RNA and main-chain or side-chain atoms of RBM38 determine the sequence-specific recognition. Our results revealed the RNA-recognition mechanism of human RBM38 and provided structural information for understanding the RNA-binding property of RBM38.

PubMed: 31860021
DOI: 10.1042/BCJ20190652

Experimental method

X-RAY DIFFRACTION (2.301 Å)