1S7A
NMR structure of the La motif of human La protein
Summary for 1S7A
| Entry DOI | 10.2210/pdb1s7a/pdb |
| Related | 1OWX 1S79 |
| NMR Information | BMRB: 6044 |
| Descriptor | Lupus La protein (1 entity in total) |
| Functional Keywords | la motif, alpha/beta, winged helix domain, rna binding protein, translation |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus (Probable): P05455 |
| Total number of polymer chains | 1 |
| Total formula weight | 12020.79 |
| Authors | Alfano, C.,Sanfelice, D.,Babon, J.,Kelly, G.,Jacks, A.,Curry, S.,Conte, M.R. (deposition date: 2004-01-29, release date: 2004-04-06, Last modification date: 2024-05-22) |
| Primary citation | Alfano, C.,Sanfelice, D.,Babon, J.,Kelly, G.,Jacks, A.,Curry, S.,Conte, M.R. Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein. Nat.Struct.Mol.Biol., 11:323-329, 2004 Cited by PubMed Abstract: The La protein is a conserved component of eukaryotic ribonucleoprotein complexes that binds the 3' poly(U)-rich elements of nascent RNA polymerase III (pol III) transcripts to assist folding and maturation. This specific recognition is mediated by the N-terminal domain (NTD) of La, which comprises a La motif and an RNA recognition motif (RRM). We have determined the solution structures of both domains and show that the La motif adopts an alpha/beta fold that comprises a winged-helix motif elaborated by the insertion of three helices. Chemical shift mapping experiments show that these insertions are involved in RNA interactions. They further delineate a distinct surface patch on each domain-containing both basic and aromatic residues-that interacts with RNA and accounts for the cooperative binding of short oligonucleotides exhibited by the La NTD. PubMed: 15004549DOI: 10.1038/nsmb747 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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