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| | <StructureSection load='5c1v' size='340' side='right'caption='[[5c1v]], [[Resolution|resolution]] 3.35Å' scene=''> | | <StructureSection load='5c1v' size='340' side='right'caption='[[5c1v]], [[Resolution|resolution]] 3.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c1v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C1V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C1V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c1v]] 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=5C1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C1V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPP3CA, CALNA, CNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5c1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c1v OCA], [https://pdbe.org/5c1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c1v RCSB], [https://www.ebi.ac.uk/pdbsum/5c1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c1v ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></td></tr>
| + | |
| - | <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=5c1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c1v OCA], [http://pdbe.org/5c1v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c1v RCSB], [http://www.ebi.ac.uk/pdbsum/5c1v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c1v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PP2BA_HUMAN PP2BA_HUMAN]] Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.<ref>PMID:15671020</ref> <ref>PMID:18838687</ref> | + | [https://www.uniprot.org/uniprot/PP2BA_HUMAN PP2BA_HUMAN] Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.<ref>PMID:15671020</ref> <ref>PMID:18838687</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoprotein phosphatase]]
| + | [[Category: Aparicio D]] |
| - | [[Category: Aparicio, D]] | + | [[Category: Aranguren-Ibanez A]] |
| - | [[Category: Aranguren-Ibanez, A]] | + | [[Category: Fita I]] |
| - | [[Category: Fita, I]] | + | [[Category: Guasch A]] |
| - | [[Category: Guasch, A]] | + | [[Category: Perez-Luque R]] |
| - | [[Category: Perez-Luque, R]] | + | [[Category: Perez-Riba M]] |
| - | [[Category: Perez-Riba, M]] | + | |
| - | [[Category: 4-layer sandwich]]
| + | |
| - | [[Category: Calcium binding]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Serine/threonine phosphatase]]
| + | |
| Structural highlights
Function
PP2BA_HUMAN Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.[1] [2]
Publication Abstract from PubMed
A limited repertoire of PPP family of serine/threonine phosphatases with a highly conserved catalytic domain acts on thousands of protein targets to orchestrate myriad central biological roles. A major structural reorganization of human calcineurin, a ubiquitous Ser/Thr PPP regulated by calcium and calmodulin and targeted by immunosuppressant drugs cyclosporin A and FK506, is unveiled here. The new conformation involves trans- to cis-isomerization of proline in the SAPNY sequence, highly conserved across PPPs, and remodels the main regulatory site where NFATc transcription factors bind. Transitions between cis- and trans-conformations may involve peptidyl prolyl isomerases such as cyclophilin A and FKBP12, which are known to physically interact with and modulate calcineurin even in the absence of immunosuppressant drugs. Alternative conformations in PPPs provide a new perspective on interactions with substrates and other protein partners and may foster development of more specific inhibitors as drug candidates.
Calcineurin Undergoes a Conformational Switch Evoked via Peptidyl-Prolyl Isomerization.,Guasch A, Aranguren-Ibanez A, Perez-Luque R, Aparicio D, Martinez-Hoyer S, Mulero MC, Serrano-Candelas E, Perez-Riba M, Fita I PLoS One. 2015 Aug 6;10(8):e0134569. doi: 10.1371/journal.pone.0134569., eCollection 2015. PMID:26248042[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wang Y, Shibasaki F, Mizuno K. Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin. J Biol Chem. 2005 Apr 1;280(13):12683-9. Epub 2005 Jan 24. PMID:15671020 doi:M411494200
- ↑ Cereghetti GM, Stangherlin A, Martins de Brito O, Chang CR, Blackstone C, Bernardi P, Scorrano L. Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria. Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15803-8. doi:, 10.1073/pnas.0808249105. Epub 2008 Oct 6. PMID:18838687 doi:10.1073/pnas.0808249105
- ↑ Guasch A, Aranguren-Ibanez A, Perez-Luque R, Aparicio D, Martinez-Hoyer S, Mulero MC, Serrano-Candelas E, Perez-Riba M, Fita I. Calcineurin Undergoes a Conformational Switch Evoked via Peptidyl-Prolyl Isomerization. PLoS One. 2015 Aug 6;10(8):e0134569. doi: 10.1371/journal.pone.0134569., eCollection 2015. PMID:26248042 doi:http://dx.doi.org/10.1371/journal.pone.0134569
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