5c1v

From Proteopedia

(Difference between revisions)

Current revision

CRYSTAL STRUCTURE ANALYSIS OF CATALYTIC SUBUNIT OF HUMAN CALCINEURIN

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:	, ,
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.^[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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5c1v"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE ANALYSIS OF CATALYTIC SUBUNIT OF HUMAN CALCINEURIN==
-<StructureSection load='5c1v' size='340' side='right' caption='[[5c1v]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
+<StructureSection load='5c1v' size='340' side='right'caption='[[5c1v]], [[Resolution|resolution]] 3.35&Aring;' 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>
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35&#8491;</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='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='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>
+<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>
 </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>
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5c1v" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Calcineurin 3D structures|Calcineurin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Phosphoprotein phosphatase]]
+[[Category: Homo sapiens]]
-[[Category: Aparicio, D]]
+[[Category: Large Structures]]
-[[Category: Aranguren-Ibanez, A]]
+[[Category: Aparicio D]]
-[[Category: Fita, I]]
+[[Category: Aranguren-Ibanez A]]
-[[Category: Guasch, A]]
+[[Category: Fita I]]
-[[Category: Perez-Luque, R]]
+[[Category: Guasch A]]
-[[Category: Perez-Riba, M]]
+[[Category: Perez-Luque R]]
-[[Category: 4-layer sandwich]]
+[[Category: Perez-Riba M]]
-[[Category: Calcium binding]]
-[[Category: Hydrolase]]
-[[Category: Serine/threonine phosphatase]]

5c1v

From Proteopedia

Current revision

CRYSTAL STRUCTURE ANALYSIS OF CATALYTIC SUBUNIT OF HUMAN CALCINEURIN

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox