6ROL
Structure of IMP2 KH34 domains
Summary for 6ROL
| Entry DOI | 10.2210/pdb6rol/pdb |
| Descriptor | Insulin-like growth factor 2 mRNA-binding protein 2, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | specificity, rna binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 75902.36 |
| Authors | Bhaskar, V.,Biswas, J.,Singer, R.H.,Chao, J.A. (deposition date: 2019-05-13, release date: 2019-10-16, Last modification date: 2024-01-24) |
| Primary citation | Biswas, J.,Patel, V.L.,Bhaskar, V.,Chao, J.A.,Singer, R.H.,Eliscovich, C. The structural basis for RNA selectivity by the IMP family of RNA-binding proteins. Nat Commun, 10:4440-4440, 2019 Cited by PubMed Abstract: The IGF2 mRNA-binding proteins (ZBP1/IMP1, IMP2, IMP3) are highly conserved post-transcriptional regulators of RNA stability, localization and translation. They play important roles in cell migration, neural development, metabolism and cancer cell survival. The knockout phenotypes of individual IMP proteins suggest that each family member regulates a unique pool of RNAs, yet evidence and an underlying mechanism for this is lacking. Here, we combine systematic evolution of ligands by exponential enrichment (SELEX) and NMR spectroscopy to demonstrate that the major RNA-binding domains of the two most distantly related IMPs (ZBP1 and IMP2) bind to different consensus sequences and regulate targets consistent with their knockout phenotypes and roles in disease. We find that the targeting specificity of each IMP is determined by few amino acids in their variable loops. As variable loops often differ amongst KH domain paralogs, we hypothesize that this is a general mechanism for evolving specificity and regulation of the transcriptome. PubMed: 31570709DOI: 10.1038/s41467-019-12193-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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