4f0z: Difference between revisions

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 ==Crystal Structure of Calcineurin in Complex with the Calcineurin-Inhibiting Domain of the African Swine Fever Virus Protein A238L==
-<StructureSection load='4f0z' size='340' side='right' caption='[[4f0z]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+<StructureSection load='4f0z' size='340' side='right'caption='[[4f0z]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4f0z]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Asfm2 Asfm2] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F0Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F0Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4f0z]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/African_swine_fever_virus_Malawi_LIL_20/1 African swine fever virus Malawi LIL 20/1] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F0Z FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aui|1aui]], [[2p6b|2p6b]], [[1mf8|1mf8]], [[1tco|1tco]], [[1m63|1m63]], [[3ll8|3ll8]]</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=4f0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f0z OCA], [https://pdbe.org/4f0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f0z RCSB], [https://www.ebi.ac.uk/pdbsum/4f0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f0z ProSAT]</span></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]), PPP3R1, CNA2, CNB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), 5EL, Mal-047, Ordered Locus Name: Mal-047 ORF Name: 5EL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10500 ASFM2])</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=4f0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f0z OCA], [http://pdbe.org/4f0z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f0z RCSB], [http://www.ebi.ac.uk/pdbsum/4f0z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f0z 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>  [[http://www.uniprot.org/uniprot/VF238_ASFM2 VF238_ASFM2]] Inhibits activation of the NF-kappa-B transcription factor by preventing binding of NF-kappa-B subunits RELA and NFKB3 to DNA. Inhibits also the activity of the calcium/calmodulin-regulated phosphatase calcineurin (By similarity). [[http://www.uniprot.org/uniprot/CANB1_HUMAN CANB1_HUMAN]] Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
+[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 ==
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 ==See Also==
-*[[Calcineurin|Calcineurin]]
+*[[Calcineurin 3D structures|Calcineurin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Asfm2]]
+[[Category: African swine fever virus Malawi LIL 20/1]]
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Phosphoprotein phosphatase]]
+[[Category: Large Structures]]
-[[Category: Grigoriu, S]]
+[[Category: Grigoriu S]]
-[[Category: Page, R]]
+[[Category: Page R]]
-[[Category: Peti, W]]
+[[Category: Peti W]]
-[[Category: Calcineurin inhibition]]
-[[Category: Calcium signaling]]
-[[Category: Calmodulin]]
-[[Category: Ef-hand]]
-[[Category: Heart]]
-[[Category: Hydrolase-protein binding complex]]
-[[Category: Ion channel]]
-[[Category: Lxvp]]
-[[Category: Nfat]]
-[[Category: Nucleus]]
-[[Category: Phosphatase]]
-[[Category: Pxixit]]
-[[Category: Rcan]]
-[[Category: Skeletal muscle]]
-[[Category: T-cell activation]]
-[[Category: Transcription regulation]]