2f2d: Difference between revisions

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 ==Solution structure of the FK506-binding domain of human FKBP38==
-<StructureSection load='2f2d' size='340' side='right'caption='[[2f2d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2f2d' size='340' side='right'caption='[[2f2d]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2f2d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F2D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2f2d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F2D FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP8, FKBP38 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2f2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f2d OCA], [https://pdbe.org/2f2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f2d RCSB], [https://www.ebi.ac.uk/pdbsum/2f2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f2d ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/FKBP8_HUMAN FKBP8_HUMAN]] Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis.<ref>PMID:12510191</ref> <ref>PMID:16176796</ref> <ref>PMID:15757646</ref>
+[https://www.uniprot.org/uniprot/FKBP8_HUMAN FKBP8_HUMAN] Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis.<ref>PMID:12510191</ref> <ref>PMID:16176796</ref> <ref>PMID:15757646</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Edlich, F]]
+[[Category: Edlich F]]
-[[Category: Fischer, G]]
+[[Category: Fischer G]]
-[[Category: Jarczowski, F]]
+[[Category: Jarczowski F]]
-[[Category: Luecke, C]]
+[[Category: Luecke C]]
-[[Category: Maestre-Martinez, M]]
+[[Category: Maestre-Martinez M]]
-[[Category: Weiwad, M]]
+[[Category: Weiwad M]]
-[[Category: Beta half-barrel]]
-[[Category: Immunophilin]]
-[[Category: Isomerase]]
-[[Category: Ppiase]]