4BWS
Crystal structure of the heterotrimer of PQBP1, U5-15kD and U5-52kD.
Summary for 4BWS
| Entry DOI | 10.2210/pdb4bws/pdb |
| Related | 4BWQ |
| Descriptor | THIOREDOXIN-LIKE PROTEIN 4A, POLYGLUTAMINE-BINDING PROTEIN 1, CD2 ANTIGEN CYTOPLASMIC TAIL-BINDING PROTEIN 2, ... (4 entities in total) |
| Functional Keywords | transcription, neurodegenerative disorders |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Cellular location | Nucleus: P83876 O60828 Cytoplasm: O95400 |
| Total number of polymer chains | 6 |
| Total formula weight | 58203.60 |
| Authors | Mizuguchi, M.,Obita, T.,Serita, T.,Kojima, R.,Morimoto, T.,Nabeshima, Y.,Okazawa, H. (deposition date: 2013-07-04, release date: 2014-04-30, Last modification date: 2023-12-20) |
| Primary citation | Mizuguchi, M.,Obita, T.,Serita, T.,Kojima, R.,Nabeshima, Y.,Okazawa, H. Mutations in the Pqbp1 Gene Prevent its Interaction with the Spliceosomal Protein U5-15Kd. Nat.Commun., 5:3822-, 2014 Cited by PubMed Abstract: A loss-of-function of polyglutamine tract-binding protein 1 (PQBP1) induced by frameshift mutations is believed to cause X-linked mental retardation. However, the mechanism by which structural changes in PQBP1 lead to mental retardation is unknown. Here we present the crystal structure of a C-terminal fragment of PQBP1 in complex with the spliceosomal protein U5-15 kD. The U5-15 kD hydrophobic groove recognizes a YxxPxxVL motif in PQBP1, and mutations within this motif cause a loss-of-function phenotype of PQBP1 in vitro. The YxxPxxVL motif is absent in all PQBP1 frameshift mutants seen in cases of mental retardation. These results suggest a mechanism by which the loss of the YxxPxxVL motif could lead to the functional defects seen in this type of mental retardation. PubMed: 24781215DOI: 10.1038/NCOMMS4822 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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