6i42
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the alpha-Synuclein PreNAC/Cyclophilin A-complex== | |
| + | <StructureSection load='6i42' size='340' side='right'caption='[[6i42]], [[Resolution|resolution]] 1.38Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6i42]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I42 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.38Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6i42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i42 OCA], [https://pdbe.org/6i42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i42 RCSB], [https://www.ebi.ac.uk/pdbsum/6i42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i42 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Peptidylprolyl isomerases (PPIases) catalyze cis/trans isomerization of prolines. The PPIase CypA colocalizes with the Parkinson's disease (PD)-associated protein alpha-synuclein in cells and interacts with alpha-synuclein oligomers. Herein, we describe atomic insights into the molecular details of the alpha-synuclein/CypA interaction. NMR spectroscopy shows that CypA catalyzes isomerization of proline 128 in the C-terminal domain of alpha-synuclein. Strikingly, we reveal a second CypA-binding site formed by the hydrophobic sequence (47) GVVHGVATVA(56) , termed PreNAC. The 1.38 A crystal structure of the CypA/PreNAC complex displays a contact between alanine 53 of alpha-synuclein and glutamine 111 in the catalytic pocket of CypA. Mutation of alanine 53 to glutamate, as found in patients with early-onset PD, weakens the interaction of alpha-synuclein with CypA. Our study provides high-resolution insights into the structure of the PD-associated protein alpha-synuclein in complex with the most abundant cellular cyclophilin. | ||
| - | + | The Molecular Basis of the Interaction of Cyclophilin A with alpha-Synuclein.,Favretto F, Baker JD, Strohaker T, Andreas LB, Blair LJ, Becker S, Zweckstetter M Angew Chem Int Ed Engl. 2019 Dec 12. doi: 10.1002/anie.201914878. PMID:31830361<ref>PMID:31830361</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6i42" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Alpha-synuclein|Alpha-synuclein]] | ||
| + | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Becker S]] | ||
| + | [[Category: Favretto F]] | ||
| + | [[Category: Zweckstetter M]] | ||
Current revision
Structure of the alpha-Synuclein PreNAC/Cyclophilin A-complex
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