5c1v
From Proteopedia
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| - | ''' | + | ==CRYSTAL STRUCTURE ANALYSIS OF CATALYTIC SUBUNIT OF HUMAN CALCINEURIN== |
| + | <StructureSection load='5c1v' size='340' side='right' caption='[[5c1v]], [[Resolution|resolution]] 3.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5c1v]] is a 2 chain structure. 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> | ||
| + | </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> | ||
| + | <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]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:26248042</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5c1v" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Phosphoprotein phosphatase]] | ||
| + | [[Category: Aparicio, D]] | ||
[[Category: Aranguren-Ibanez, A]] | [[Category: Aranguren-Ibanez, A]] | ||
| + | [[Category: Fita, I]] | ||
[[Category: Guasch, A]] | [[Category: Guasch, A]] | ||
| + | [[Category: Perez-Luque, R]] | ||
[[Category: Perez-Riba, M]] | [[Category: Perez-Riba, M]] | ||
| - | [[Category: | + | [[Category: 4-layer sandwich]] |
| - | [[Category: | + | [[Category: Calcium binding]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| + | [[Category: Serine/threonine phosphatase]] | ||
Revision as of 15:41, 3 February 2016
CRYSTAL STRUCTURE ANALYSIS OF CATALYTIC SUBUNIT OF HUMAN CALCINEURIN
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