Summary information and primary citation

PDB-id
6jvx; SNAP-derived features in text and JSON formats; DNAproDB
Class
RNA binding protein-RNA
Method
X-ray (2.301 Å)
Summary
Crystal structure of rbm38 in complex with RNA
Reference
Qian K, Li M, Wang J, Zhang M, Wang M (2020): "Structural basis for mRNA recognition by human RBM38." Biochem.J., 477, 161-172. doi: 10.1042/BCJ20190652.
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.

Cartoon-block schematics in six views (download the tarball)

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