1QM9
NMR, REPRESENTATIVE STRUCTURE
Summary for 1QM9
| Entry DOI | 10.2210/pdb1qm9/pdb |
| NMR Information | BMRB: 5409 |
| Descriptor | POLYPYRIMIDINE TRACT-BINDING PROTEIN (1 entity in total) |
| Functional Keywords | ribonucleoprotein, polypyrimidine tract binding protein, rnp, rna, spicing, translation |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Nucleus: P26599 |
| Total number of polymer chains | 1 |
| Total formula weight | 22117.32 |
| Authors | Conte, M.R.,Grune, T.,Curry, S.,Matthews, S. (deposition date: 1999-09-22, release date: 2000-07-03, Last modification date: 2024-05-15) |
| Primary citation | Conte, M.R.,Grune, T.,Kelly, G.,Ladas, A.,Matthews, S.,Curry, S. Structure of Tandem RNA Recognition Motifs from Polypyrimidine Tract Binding Protein Reveals Novel Features of the Rrm Fold Embo J., 19:3132-, 2000 Cited by PubMed Abstract: Polypyrimidine tract binding protein (PTB), an RNA binding protein containing four RNA recognition motifs (RRMs), is involved in both pre-mRNA splicing and translation initiation directed by picornaviral internal ribosome entry sites. Sequence comparisons previously indicated that PTB is a non-canonical RRM protein. The solution structure of a PTB fragment containing RRMs 3 and 4 shows that the protein consists of two domains connected by a long, flexible linker. The two domains tumble independently in solution, having no fixed relative orientation. In addition to the betaalphabetabetaalphabeta topology, which is characteristic of RRM domains, the C-terminal extension of PTB RRM-3 incorporates an unanticipated fifth beta-strand, which extends the RNA binding surface. The long, disordered polypeptide connecting beta4 and beta5 in RRM-3 is poised above the RNA binding surface and is likely to contribute to RNA recognition. Mutational analyses show that both RRM-3 and RRM-4 contribute to RNA binding specificity and that, despite its unusual sequence, PTB binds RNA in a manner akin to that of other RRM proteins. PubMed: 10856256DOI: 10.1093/EMBOJ/19.12.3132 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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