1p5q

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[[Image:1p5q.jpg|left|200px]]<br /><applet load="1p5q" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1p5q, resolution 2.8&Aring;" />
 
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'''Crystal Structure of FKBP52 C-terminal Domain'''<br />
 
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==Overview==
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==Crystal Structure of FKBP52 C-terminal Domain==
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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.
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<StructureSection load='1p5q' size='340' side='right'caption='[[1p5q]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1p5q]] is a 3 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=1P5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P5Q FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5q OCA], [https://pdbe.org/1p5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p5q RCSB], [https://www.ebi.ac.uk/pdbsum/1p5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p5q ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p5/1p5q_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1p5q ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1P5Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5Q OCA].
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*[[FKBP 3D structures|FKBP 3D structures]]
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== References ==
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==Reference==
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<references/>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15159550 15159550]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Ding Y]]
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[[Category: Ding, Y.]]
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[[Category: Li P]]
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[[Category: Li, P.]]
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[[Category: Lou Z]]
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[[Category: Lou, Z.]]
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[[Category: Rao Z]]
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[[Category: Rao, Z.]]
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[[Category: Shen B]]
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[[Category: Shen, B.]]
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[[Category: Shu C]]
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[[Category: Shu, C.]]
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[[Category: Wu B]]
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[[Category: Wu, B.]]
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[[Category: SO4]]
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[[Category: isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:38:55 2008''
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Current revision

Crystal Structure of FKBP52 C-terminal Domain

PDB ID 1p5q

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