5c1v

CRYSTAL STRUCTURE ANALYSIS OF CATALYTIC SUBUNIT OF HUMAN CALCINEURIN

spinqualitylabelsall models 5c1v, resolution 3.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5c1v 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. Method: X-ray diffraction, Resolution 3.35Å Ligands: FE, PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Calcineurin 3D structures

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