2MQM
Structural Investigation of hnRNP L
Summary for 2MQM
| Entry DOI | 10.2210/pdb2mqm/pdb |
| Related | 2MQL 2MQN 2MQO 2MQP 2MQQ |
| NMR Information | BMRB: 25039 |
| Descriptor | Protein Hnrnpl (1 entity in total) |
| Functional Keywords | protein, rrm, rna binding protein |
| Biological source | Rattus norvegicus (rat) |
| Total number of polymer chains | 1 |
| Total formula weight | 13079.71 |
| Authors | Blatter, M.,Allain, F. (deposition date: 2014-06-24, release date: 2015-05-06, Last modification date: 2024-05-15) |
| Primary citation | Blatter, M.,Dunin-Horkawicz, S.,Grishina, I.,Maris, C.,Thore, S.,Maier, T.,Bindereif, A.,Bujnicki, J.M.,Allain, F.H. The Signature of the Five-Stranded vRRM Fold Defined by Functional, Structural and Computational Analysis of the hnRNP L Protein. J.Mol.Biol., 427:3001-3022, 2015 Cited by PubMed Abstract: The RNA recognition motif (RRM) is the far most abundant RNA binding domain. In addition to the typical β1α1β2β3α2β4 fold, various sub-structural elements have been described and reportedly contribute to the high functional versatility of RRMs. The heterogeneous nuclear ribonucleoprotein L (hnRNP L) is a highly abundant protein of 64 kDa comprising four RRM domains. Involved in many aspects of RNA metabolism, hnRNP L specifically binds to RNAs containing CA repeats or CA-rich clusters. However, a comprehensive structural description of hnRNP L including its sub-structural elements is missing. Here, we present the structural characterization of the RRM domains of hnRNP L and demonstrate their function in repressing exon 4 of SLC2A2. By comparison of the sub-structural elements between the two highly similar paralog families of hnRNP L and PTB, we defined signatures underlying interacting C-terminal coils (ICCs), the RRM34 domain interaction and RRMs with a C-terminal fifth β-strand, a variation we denoted vRRMs. Furthermore, computational analysis revealed new putative ICC-containing RRM families and allowed us to propose an evolutionary scenario explaining the origins of the ICC and fifth β-strand sub-structural extensions. Our studies provide insights of domain requirements in alternative splicing mediated by hnRNP L and molecular descriptions for the sub-structural elements. In addition, the analysis presented may help to classify other abundant RRM extensions and to predict structure-function relationships. PubMed: 26051023DOI: 10.1016/j.jmb.2015.05.020 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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