6KOR

Crystal structure of the RRM domain of SYNCRIP

Summary for 6KOR

• Entry DOI: 10.2210/pdb6kor/pdb
• Descriptor: Heterogeneous nuclear ribonucleoprotein Q (2 entities in total)
• Functional Keywords: rna recognition motif, rna binding protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 22243.46

Authors

Chen, Y.,Chan, J.,Chen, W.,Jobichen, C. (deposition date: 2019-08-12, release date: 2020-01-22, Last modification date: 2023-11-22)

Primary citation

Chen, Y.,Chan, J.,Chen, W.,Li, J.,Sun, M.,Kannan, G.S.,Mok, Y.K.,Yuan, Y.A.,Jobichen, C.
SYNCRIP, a new player in pri-let-7a processing.
Rna, 26:290-305, 2020

PubMed Abstract: microRNAs (miRNAs), a class of small and endogenous molecules that control gene expression, are broadly involved in biological processes. Although a number of cofactors that assist or antagonize let-7 miRNA biogenesis are well-established, more auxiliary factors remain to be investigated. Here, we identified SYNCRIP (Synaptotagmin Binding Cytoplasmic RNA Interacting Protein) as a new player for let-7a miRNA. SYNCRIP interacts with pri-let-7a both in vivo and in vitro. Knockdown of SYNCRIP impairs, while overexpression of SYNCRIP promotes, the expression of let-7a miRNA. A broad miRNA profiling analysis revealed that silencing of SYNCRIP regulates the expression of a set of mature miRNAs positively or negatively. In addition, SYNCRIP is associated with microprocessor complex and promotes the processing of pri-let-7a. Strikingly, the terminal loop of pri-let-7a was shown to be the main contributor for its interaction with SYNCRIP. Functional studies demonstrated that the SYNCRIP RRM2-3 domain can promote the processing of pri-let-7a. Structure-based alignment of RRM2-3 with other RNA binding proteins identified the residues likely to participate in protein-RNA interactions. Taken together, these findings suggest the promising role that SYNCRIP plays in miRNA regulation, thus providing insights into the function of SYNCRIP in eukaryotic development.

PubMed: 31907208
DOI: 10.1261/rna.072959.119

Experimental method

X-RAY DIFFRACTION (2.602 Å)