6i42: Difference between revisions
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==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]] | |||
