2LRS
The second dsRBD domain from A. thaliana DICER-LIKE 1
Summary for 2LRS
| Entry DOI | 10.2210/pdb2lrs/pdb |
| NMR Information | BMRB: 18393 |
| Descriptor | Endoribonuclease Dicer homolog 1 (1 entity in total) |
| Functional Keywords | mirna, rna binding, hydrolase |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
| Cellular location | Nucleus: Q9SP32 |
| Total number of polymer chains | 1 |
| Total formula weight | 7961.23 |
| Authors | Burdisso, P.,Suarez, I.,Bersch, B.,Bologna, N.,Palatnik, J.,Boisbouvier, J.,Rasia, R. (deposition date: 2012-04-12, release date: 2013-01-23, Last modification date: 2024-05-01) |
| Primary citation | Burdisso, P.,Suarez, I.P.,Bologna, N.G.,Palatnik, J.F.,Bersch, B.,Rasia, R.M. Second Double-Stranded RNA Binding Domain of Dicer-like Ribonuclease 1: Structural and Biochemical Characterization. Biochemistry, 51:10159-10166, 2012 Cited by PubMed Abstract: Dicer-like ribonuclease III enzymes are involved in different paths related to RNA silencing in plants. Little is known about the structural aspects of these processes. Here we present a structural characterization of the second double-stranded RNA binding domain (dsRBD) of DCL1, which is presumed to participate in pri-micro-RNA recognition and subcellular localization of this protein. We determined the solution structure and found that it has a canonical fold but bears some variation with respect to other homologous domains. We also found that this domain binds both double-stranded RNA and double-stranded DNA, in contrast to most dsRBDs. Our characterization shows that this domain likely has functions other than substrate recognition and binding. PubMed: 23194006DOI: 10.1021/bi301247r PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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