2bn5

From Proteopedia

Revision as of 06:43, 21 November 2007

P-ELEMENT SOMATIC INHIBITOR PROTEIN COMPLEX WITH U1-70K PROLINE-RICH PEPTIDE

Overview

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.

About this Structure

2BN5 is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Structural basis of the interaction between P-element somatic inhibitor and U1-70k essential for the alternative splicing of P-element transposase., Ignjatovic T, Yang JC, Butler J, Neuhaus D, Nagai K, J Mol Biol. 2005 Aug 5;351(1):52-65. PMID:15990112

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