3ey6: Difference between revisions

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==Crystal structure of the FK506-binding domain of human FKBP38==
==Crystal structure of the FK506-binding domain of human FKBP38==
<StructureSection load='3ey6' size='340' side='right' caption='[[3ey6]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
<StructureSection load='3ey6' size='340' side='right'caption='[[3ey6]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ey6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EY6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ey6]] is a 1 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=3EY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EY6 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f2d|2f2d]], [[2awg|2awg]]</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]] 1.05&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP38, FKBP8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [https://pdbe.org/3ey6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ey6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ey6 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [http://pdbe.org/3ey6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ey6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ey6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ey/3ey6_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ey/3ey6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
*[[FK506 binding protein|FK506 binding protein]]
*[[FKBP 3D structures|FKBP 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Large Structures]]
[[Category: Edlich, F]]
[[Category: Edlich F]]
[[Category: Fischer, G]]
[[Category: Fischer G]]
[[Category: Luecke, C]]
[[Category: Luecke C]]
[[Category: Maestre-Martinez, M]]
[[Category: Maestre-Martinez M]]
[[Category: Neumann, P]]
[[Category: Neumann P]]
[[Category: Parthier, C]]
[[Category: Parthier C]]
[[Category: Stubbs, M T]]
[[Category: Stubbs MT]]
[[Category: Apoptosis]]
[[Category: Beta half-barrel]]
[[Category: Host-virus interaction]]
[[Category: Immunophilin]]
[[Category: Isomerase]]
[[Category: Membrane]]
[[Category: Mitochondrion]]
[[Category: Phosphoprotein]]
[[Category: Ppiase]]
[[Category: Rotamase]]
[[Category: Tpr repeat]]
[[Category: Transmembrane]]

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