1UN6
THE CRYSTAL STRUCTURE OF A ZINC FINGER - RNA COMPLEX REVEALS TWO MODES OF MOLECULAR RECOGNITION
Summary for 1UN6
Entry DOI | 10.2210/pdb1un6/pdb |
Related | 1TF3 1TF6 |
Descriptor | TRANSCRIPTION FACTOR IIIA, 5S RIBOSOMAL RNA, ZINC ION, ... (5 entities in total) |
Functional Keywords | rna-binding protein/rna, complex(zinc finger-rna), tfiiia, 5s ribosomal rna, zinc finger, rna-protein complex, x. laevis, transcription regulation, rna-binding, dna-binding, nuclear protein, rna-binding protein-rna complex |
Biological source | XENOPUS LAEVIS (AFRICAN CLAWED FROG) More |
Cellular location | Nucleus: P03001 |
Total number of polymer chains | 5 |
Total formula weight | 71156.30 |
Authors | Lu, D.,Searles, M.A.,Klug, A. (deposition date: 2003-09-04, release date: 2003-11-20, Last modification date: 2024-05-08) |
Primary citation | Lu, D.,Searles, M.A.,Klug, A. Crystal Structure of a Zinc-Finger-RNA Complex Reveals Two Modes of Molecular Recognition Nature, 426:96-, 2003 Cited by PubMed Abstract: Zinc-finger proteins of the classical Cys2His2 type are the most frequently used class of transcription factor and account for about 3% of genes in the human genome. The zinc-finger motif was discovered during biochemical studies on the transcription factor TFIIIA, which regulates the 5S ribosomal RNA genes of Xenopus laevis. Zinc-fingers mostly interact with DNA, but TFIIIA binds not only specifically to the promoter DNA, but also to 5S RNA itself. Increasing evidence indicates that zinc-fingers are more widely used to recognize RNA. There have been numerous structural studies on DNA binding, but none on RNA binding by zinc-finger proteins. Here we report the crystal structure of a three-finger complex with 61 bases of RNA, derived from the central regions of the complete nine-finger TFIIIA-5S RNA complex. The structure reveals two modes of zinc-finger binding, both of which differ from that in common use for DNA: first, the zinc-fingers interact with the backbone of a double helix; and second, the zinc-fingers specifically recognize individual bases positioned for access in otherwise intricately folded 'loop' regions of the RNA. PubMed: 14603324DOI: 10.1038/NATURE02088 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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