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2x7k

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Revision as of 14:42, 24 December 2014

THE CRYSTAL STRUCTURE OF PPIL1 IN COMPLEX WITH CYCLOSPORINE A SUGGESTS A BINDING MODE FOR SKIP

Structural highlights

2x7k is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:	, , , , ,
Related:	1bck, 1c5f, 1csa, 1cwa, 1cwb, 1cwc, 1cwf, 1cwh, 1cwi, 1cwj, 1cwk, 1cwl, 1cwm, 1cwo, 1cya, 1cyb, 1cyn, 1ikf, 1m63, 1mf8, 1mik, 1qng, 1qnh, 1xq7, 2esl, 2oju, 2poy, 2rma, 2rmb, 2rmc, 2wfj, 2x2c, 2z6w, 3bo7, 3cys, 3eov, 1xwn
Activity:	Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PPIL1_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

BACKGROUND: The removal of introns from pre-mRNA is carried out by a large macromolecular machine called the spliceosome. The peptidyl-prolyl cis/trans isomerase PPIL1 is a component of the human spliceosome and binds to the spliceosomal SKIP protein via a binding site distinct from its active site. PRINCIPAL FINDINGS: Here, we have studied the PPIL1 protein and its interaction with SKIP biochemically and by X-ray crystallography. A minimal linear binding epitope derived from the SKIP protein could be determined using a peptide array. A 36-residue region of SKIP centred on an eight-residue epitope suffices to bind PPIL1 in pull-down experiments. The crystal structure of PPIL1 in complex with the inhibitor cyclosporine A (CsA) was obtained at a resolution of 1.15 A and exhibited two bound Cd(2+) ions that enabled SAD phasing. PPIL1 residues that have previously been implicated in binding of SKIP are involved in the coordination of Cd(2+) ions in the present crystal structure. Employing the present crystal structure, the determined minimal binding epitope and previously published NMR data, a molecular docking study was performed. In the docked model of the PPIL1.SKIP interaction, a proline residue of SKIP is buried in a hydrophobic pocket of PPIL1. This hydrophobic contact is encircled by several hydrogen bonds between the SKIP peptide and PPIL1. CONCLUSION: We characterized a short, linear epitope of SKIP that is sufficient to bind the PPIL1 protein. Our data indicate that this SKIP peptide could function in recruiting PPIL1 into the core of the spliceosome. We present a molecular model for the binding mode of SKIP to PPIL1 which emphasizes the versatility of cyclophilin-type PPIases to engage in additional interactions with other proteins apart from active site contacts despite their limited surface area.

The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein.,Stegmann CM, Luhrmann R, Wahl MC PLoS One. 2010 Apr 2;5(4):e10013. PMID:20368803^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. 2006 Jun 9;281(23):15900-8. Epub 2006 Apr 4. PMID:16595688 doi:10.1074/jbc.M511155200
↑ Stegmann CM, Luhrmann R, Wahl MC. The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein. PLoS One. 2010 Apr 2;5(4):e10013. PMID:20368803 doi:10.1371/journal.pone.0010013

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x7k"

@@ Line 9: / Line 9: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x7k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x7k RCSB], [http://www.ebi.ac.uk/pdbsum/2x7k PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PPIL1_HUMAN PPIL1_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.<ref>PMID:16595688</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 35: @@
 [[Category: Homo sapiens]]
 [[Category: Peptidylprolyl isomerase]]
-[[Category: Luehrmann, R.]]
+[[Category: Luehrmann, R]]
-[[Category: Stegmann, C M.]]
+[[Category: Stegmann, C M]]
-[[Category: Wahl, M C.]]
+[[Category: Wahl, M C]]
 [[Category: Cyclosporin some]]
 [[Category: Immunosuppressant]]
 [[Category: Isomerase-cyclosporin complex]]
 [[Category: Isomerase-immunosuppressant complex]]

2x7k

From Proteopedia

Revision as of 14:42, 24 December 2014

THE CRYSTAL STRUCTURE OF PPIL1 IN COMPLEX WITH CYCLOSPORINE A SUGGESTS A BINDING MODE FOR SKIP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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