2KXF
Solution structure of the first two RRM domains of FBP-interacting repressor (FIR)
Summary for 2KXF
| Entry DOI | 10.2210/pdb2kxf/pdb |
| Related | 2KXH |
| Descriptor | Poly(U)-binding-splicing factor PUF60 (1 entity in total) |
| Functional Keywords | rrm, rna binding, protein binding |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 21927.02 |
| Authors | Cukier, C.D.,Ramos, A.,Hollingworth, D.,Diaz-Moreno, I.,Kelly, G. (deposition date: 2010-05-04, release date: 2010-08-18, Last modification date: 2024-05-01) |
| Primary citation | Cukier, C.D.,Hollingworth, D.,Martin, S.R.,Kelly, G.,Diaz-Moreno, I.,Ramos, A. Molecular basis of FIR-mediated c-myc transcriptional control. Nat.Struct.Mol.Biol., 17:1058-1064, 2010 Cited by PubMed Abstract: The far upstream element (FUSE) regulatory system promotes a peak in the concentration of c-Myc during cell cycle. First, the FBP transcriptional activator binds to the FUSE DNA element upstream of the c-myc promoter. Then, FBP recruits its specific repressor (FIR), which acts as an on/off transcriptional switch. Here we describe the molecular basis of FIR recruitment, showing that the tandem RNA recognition motifs of FIR provide a platform for independent FUSE DNA and FBP protein binding and explaining the structural basis of the reversibility of the FBP-FIR interaction. We also show that the physical coupling between FBP and FIR is modulated by a flexible linker positioned sequentially to the recruiting element. Our data explain how the FUSE system precisely regulates c-myc transcription and suggest that a small change in FBP-FIR affinity leads to a substantial effect on c-Myc concentration. PubMed: 20711187DOI: 10.1038/nsmb.1883 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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