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- | [[Image:1qz2.jpg|left|200px]] | |
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- | <!--
| + | ==Crystal Structure of FKBP52 C-terminal Domain complex with the C-terminal peptide MEEVD of Hsp90== |
- | The line below this paragraph, containing "STRUCTURE_1qz2", creates the "Structure Box" on the page.
| + | <StructureSection load='1qz2' size='340' side='right'caption='[[1qz2]], [[Resolution|resolution]] 3.00Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1qz2]] is a 5 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=1QZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QZ2 FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=1qz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qz2 OCA], [https://pdbe.org/1qz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qz2 RCSB], [https://www.ebi.ac.uk/pdbsum/1qz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qz2 ProSAT]</span></td></tr> |
- | {{STRUCTURE_1qz2| PDB=1qz2 | SCENE= }}
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/FKBP4_HUMAN FKBP4_HUMAN] Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria.<ref>PMID:1279700</ref> <ref>PMID:1376003</ref> <ref>PMID:2378870</ref> <ref>PMID:19945390</ref> <ref>PMID:21730050</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/qz/1qz2_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=1qz2 ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | '''Crystal Structure of FKBP52 C-terminal Domain complex with the C-terminal peptide MEEVD of Hsp90'''
| + | ==See Also== |
- | | + | *[[FKBP 3D structures|FKBP 3D structures]] |
- | | + | == References == |
- | ==Overview== | + | <references/> |
- | FK506-binding protein 52 (FKBP52), which binds FK506 and possesses peptidylprolyl isomerase activity, is an important immunophilin involved in the heterocomplex of steroid receptors with heat-shock protein 90. Here we report the crystal structures of two overlapped fragments [N(1-260) and C(145-459)] of FKBP52 and the complex with a C-terminal pentapeptide from heat-shock protein 90. Based on the structures of these two overlapped fragments, the complete putative structure of FKBP52 can be defined. The structure of FKBP52 is composed of two consecutive FKBP domains, a tetratricopeptide repeat domain and a short helical domain beyond the final tetratricopeptide repeat motif. Key structural differences between FKBP52 and FKBP51, including the relative orientations of the four domains and some important residue substitutions, could account for the differential functions of FKBPs.
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==About this Structure== | + | |
- | 1QZ2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZ2 OCA].
| + | |
- | | + | |
- | ==Reference==
| + | |
- | 3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex., Wu B, Li P, Liu Y, Lou Z, Ding Y, Shu C, Ye S, Bartlam M, Shen B, Rao Z, Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8348-53. Epub 2004 May 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15159550 15159550]
| + | |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
- | [[Category: Peptidylprolyl isomerase]] | + | [[Category: Large Structures]] |
- | [[Category: Protein complex]]
| + | [[Category: Ding Y]] |
- | [[Category: Ding, Y.]] | + | [[Category: Li P]] |
- | [[Category: Li, P.]] | + | [[Category: Liu Y]] |
- | [[Category: Liu, Y.]] | + | [[Category: Lou Z]] |
- | [[Category: Lou, Z.]] | + | [[Category: Rao Z]] |
- | [[Category: Rao, Z.]] | + | [[Category: Shen B]] |
- | [[Category: Shen, B.]] | + | [[Category: Shu C]] |
- | [[Category: Shu, C.]] | + | [[Category: Wu B]] |
- | [[Category: Wu, B.]] | + | |
- | [[Category: Chaperone]]
| + | |
- | [[Category: Heat shock]]
| + | |
- | [[Category: Isomerase]]
| + | |
- | [[Category: Rotamase]]
| + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:52:39 2008''
| + | |
| Structural highlights
Function
FKBP4_HUMAN Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Peattie DA, Harding MW, Fleming MA, DeCenzo MT, Lippke JA, Livingston DJ, Benasutti M. Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes. Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10974-8. PMID:1279700
- ↑ Tai PK, Albers MW, Chang H, Faber LE, Schreiber SL. Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex. Science. 1992 May 29;256(5061):1315-8. PMID:1376003
- ↑ Sanchez ER, Faber LE, Henzel WJ, Pratt WB. The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins. Biochemistry. 1990 May 29;29(21):5145-52. PMID:2378870
- ↑ Shim S, Yuan JP, Kim JY, Zeng W, Huang G, Milshteyn A, Kern D, Muallem S, Ming GL, Worley PF. Peptidyl-prolyl isomerase FKBP52 controls chemotropic guidance of neuronal growth cones via regulation of TRPC1 channel opening. Neuron. 2009 Nov 25;64(4):471-83. doi: 10.1016/j.neuron.2009.09.025. PMID:19945390 doi:10.1016/j.neuron.2009.09.025
- ↑ Gallo LI, Lagadari M, Piwien-Pilipuk G, Galigniana MD. The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress. J Biol Chem. 2011 Aug 26;286(34):30152-60. doi: 10.1074/jbc.M111.256610. Epub, 2011 Jul 5. PMID:21730050 doi:10.1074/jbc.M111.256610
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