1xwn

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Revision as of 18:05, 12 November 2007

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solution structure of cyclophilin like 1(PPIL1) and insights into its interaction with SKIP

Overview

The human PPIL1 (peptidyl prolyl isomerase-like protein 1) is a specific, component of human 35 S U5 small nuclear ribonucleoprotein particle and 45, S activated spliceosome. It is recruited by SKIP, another essential, component of 45 S activated spliceosome, into spliceosome just before the, catalytic step 1. It stably associates with SKIP, which also exists in 35, S and activated spliceosome as a nuclear matrix protein. We report here, the solution structure of PPIL1 determined by NMR spectroscopy. The, structure of PPIL1 resembles other members of the cyclophilin family and, exhibits PPIase activity. To investigate its interaction with SKIP in, vitro, we identified the SKIP contact region by GST pulldown experiments, and surface plasmon resonance. We provide direct evidence of PPIL1 stably, associated with SKIP. The dissociation constant is 1.25 x 10(-7) M for the, N-terminal peptide of SKIP-(59-129) with PPIL1. We also used chemical, shift perturbation experiments to show the possible SKIP binding interface, on PPIL1. These results illustrated that a novel cyclophilin-protein, contact mode exists in the PPIL1-SKIP complex during activation of the, spliceosome. The biological implication of this binding with spliceosome, rearrangement during activation is discussed.

About this Structure

1XWN is a Single protein structure of sequence from Homo sapiens. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.

Reference

Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP., Xu C, Zhang J, Huang X, Sun J, Xu Y, Tang Y, Wu J, Shi Y, Huang Q, Zhang Q, J Biol Chem. 2006 Jun 9;281(23):15900-8. Epub 2006 Apr 4. PMID:16595688

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