3ADL

Structure of TRBP2 and its molecule implications for miRNA processing

Summary for 3ADL

• Entry DOI: 10.2210/pdb3adl/pdb
• Related: 3ADG 3ADI 3ADJ
• Descriptor: RISC-loading complex subunit TARBP2, RNA (5'-R(P*CP*GP*CP*GP*CP*GP*CP*GP*CP*G)-3') (3 entities in total)
• Functional Keywords: trbp2, mirna processing, gene regulation-rna complex, gene regulation/rna
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q15633
• Total number of polymer chains: 3
• Total formula weight: 16345.37

Authors

Yuan, Y.A.,Chen, H.Y. (deposition date: 2010-01-22, release date: 2010-05-26, Last modification date: 2023-11-01)

Primary citation

Yang, S.W.,Chen, H.Y.,Yang, J.,Machida, S.,Chua, N.H.,Yuan, Y.A.
Structure of arabidopsis HYPONASTIC LEAVES1 and its molecular implications for miRNA processing
Structure, 18:594-605, 2010

PubMed Abstract: The Arabidopsis HYPONASTIC LEAVES1 (HYL1) is a double-stranded RNA-binding protein that forms a complex with DICER-LIKE1 (DCL1) and SERRATE to facilitate processing of primary miRNAs into microRNAs (miRNAs). However, the structural mechanisms of miRNA maturation by this complex are poorly understood. Here, we present the crystal structures of double-stranded RNA binding domains (dsRBD1 and dsRBD2) of HYL1 and HYL1 dsRBD1 (HR1)/dsRNA complex as well as human TRBP2 dsRBD2 (TR2)/dsRNA complex for comparison analysis. Structural and functional study demonstrates that both HR1 and TR2 are canonical dsRBDs for dsRNA binding, whereas HR2 of HYL1 is a non-canonical dsRBD harboring a putative dimerization interface. Domain swapping within the context of HYL1 demonstrates that TR2 can supplant the function of HR1 in vitro and in vivo. Further biochemical analyses suggest that HYL1 probably binds to the miRNA/miRNA( *) region of precursors as a dimer mediated by HR2.

PubMed: 20462493
DOI: 10.1016/j.str.2010.02.006

Experimental method

X-RAY DIFFRACTION (2.2 Å)