2awg
From Proteopedia
(Difference between revisions)
| (13 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2awg.gif|left|200px]]<br /><applet load="2awg" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2awg, resolution 1.60Å" /> | ||
| - | '''Structure of the PPIase domain of the Human FK506-binding protein 8'''<br /> | ||
| - | == | + | ==Structure of the PPIase domain of the Human FK506-binding protein 8== |
| - | + | <StructureSection load='2awg' size='340' side='right'caption='[[2awg]], [[Resolution|resolution]] 1.60Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2awg]] 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=2AWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AWG FirstGlance]. <br> |
| - | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</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=2awg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2awg OCA], [https://pdbe.org/2awg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2awg RCSB], [https://www.ebi.ac.uk/pdbsum/2awg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2awg 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> |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | [ | + | Check<jmol> |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/2awg_consurf.spt"</scriptWhenChecked> | |
| - | [[ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | + | <text>to colour the structure by Evolutionary Conservation</text> | |
| - | + | </jmolCheckbox> | |
| - | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2awg ConSurf]. | |
| - | [ | + | <div style="clear:both"></div> |
| - | [[ | + | |
| - | [ | + | |
| - | + | ||
| - | + | ==See Also== | |
| + | *[[FKBP 3D structures|FKBP 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith C]] | ||
| + | [[Category: Bochkarev A]] | ||
| + | [[Category: Davis T]] | ||
| + | [[Category: Dhe-Paganon S]] | ||
| + | [[Category: Edwards A]] | ||
| + | [[Category: Finerty P]] | ||
| + | [[Category: Mackenzie F]] | ||
| + | [[Category: Newman EM]] | ||
| + | [[Category: Sundstrom M]] | ||
| + | [[Category: Walker JR]] | ||
| + | [[Category: Weigelt J]] | ||
Current revision
Structure of the PPIase domain of the Human FK506-binding protein 8
| |||||||||||
Categories: Homo sapiens | Large Structures | Arrowsmith C | Bochkarev A | Davis T | Dhe-Paganon S | Edwards A | Finerty P | Mackenzie F | Newman EM | Sundstrom M | Walker JR | Weigelt J

