1XWN

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

Summary for 1XWN

• Entry DOI: 10.2210/pdb1xwn/pdb
• Descriptor: Peptidyl-prolyl cis-trans isomerase like 1 (1 entity in total)
• Functional Keywords: beta barrel, isomerase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 19328.96

Authors

Xu, C.,Xu, Y.,Tang, Y.,Wu, J.,Shi, Y.,Huang, Q.,Zhang, Q. (deposition date: 2004-11-01, release date: 2005-10-18, Last modification date: 2024-05-29)

Primary citation

Xu, C.,Zhang, J.,Huang, X.,Sun, J.,Xu, Y.,Tang, Y.,Wu, J.,Shi, Y.,Huang, Q.,Zhang, Q.
Solution structure of human peptidyl prolyl isomerase like protein 1 and insights into its interaction with SKIP
J.Biol.Chem., 281:15900-15908, 2006

PubMed Abstract: 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.

PubMed: 16595688
DOI: 10.1074/jbc.M511155200

Experimental method

SOLUTION NMR