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2BN6

P-Element Somatic Inhibitor Protein

Summary for 2BN6
Entry DOI10.2210/pdb2bn6/pdb
Related2BN5
DescriptorPSI (1 entity in total)
Functional Keywordssplicing, protein-protein interaction, proline-rich peptide, nuclear protein
Biological sourceDROSOPHILA MELANOGASTER (FRUIT FLY)
Total number of polymer chains1
Total formula weight3796.14
Authors
Ignjatovic, T.,Yang, J.C.,Butler, P.J.G.,Neuhaus, D.,Nagai, K. (deposition date: 2005-03-21, release date: 2005-07-06, Last modification date: 2024-05-15)
Primary citationIgnjatovic, T.,Yang, J.C.,Butler, J.,Neuhaus, D.,Nagai, K.
Structural Basis of the Interaction between P-Element Somatic Inhibitor and U1-70K Essential for the Alternative Splicing of P-Element Transposase.
J.Mol.Biol., 351:52-, 2005
Cited by
PubMed Abstract: P-element transposition in Drosophila is regulated by tissue-specific alternative splicing of the P-element transposase pre-mRNA. In somatic cells, the P-element somatic inhibitor (PSI) protein binds to exon 3 of the pre-mRNA and recruits U1 small nuclear ribonucleoprotein (snRNP) to the F1 pseudo-splice site. This abrogates binding of U1 snRNP to the genuine 5' splice site, thereby preventing excision of the third intron. Two homologous short sequences, referred to as the A and B boxes, near the C terminus of PSI bind to U1-70k protein within U1 snRNP. We have now mapped the AB box-binding site of U1-70k to a short proline-rich sequence at the C terminus. Our NMR study shows that the B box forms an anti-parallel helical hairpin in which four highly conserved aromatic residues form a cluster on one face of the first helix. This hydrophobic cluster interacts extensively with the proline-rich region of the U1-70k protein.
PubMed: 15990112
DOI: 10.1016/J.JMB.2005.04.077
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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