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[[Image:1kt1.gif|left|200px]]


{{Structure
==Structure of the Large FKBP-like Protein, FKBP51, Involved in Steroid Receptor Complexes==
|PDB= 1kt1 |SIZE=350|CAPTION= <scene name='initialview01'>1kt1</scene>, resolution 2.80&Aring;
<StructureSection load='1kt1' size='340' side='right'caption='[[1kt1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
<table><tr><td colspan='2'>[[1kt1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saimiri_boliviensis Saimiri boliviensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KT1 FirstGlance]. <br>
|ACTIVITY= [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]  
</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>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1kt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kt1 OCA], [https://pdbe.org/1kt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kt1 RCSB], [https://www.ebi.ac.uk/pdbsum/1kt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kt1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FKBP5_SAIBB FKBP5_SAIBB] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP (By similarity). Interacts with the glucocorticoid receptor and modulates its response to glucocorticoids.<ref>PMID:11089542</ref> <ref>PMID:12538866</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/kt/1kt1_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=1kt1 ConSurf].
<div style="clear:both"></div>


'''Structure of the Large FKBP-like Protein, FKBP51, Involved in Steroid Receptor Complexes'''
==See Also==
 
*[[FKBP 3D structures|FKBP 3D structures]]
 
== References ==
==Overview==
<references/>
The ability to bind immunosuppressive drugs such as cyclosporin and FK506 defines the immunophilin family of proteins, and the FK506-binding proteins form the FKBP subfamily of immunophilins. Some FKBPs, notably FKBP12 (the 12-kDa FK506-binding protein), have defined roles in regulating ion channels or cell signaling, and well established structures. Other FKBPs, especially the larger ones, participate in important biological processes, but their exact roles and the structural bases for these roles are poorly defined. FKBP51 (the 51-kDa FKBP) associates with heat shock protein 90 (Hsp90) and appears in functionally mature steroid receptor complexes. In New World monkeys, FKBP51 has been implicated in cortisol resistance. We report here the x-ray structures of human FKBP51, to 2.7 A, and squirrel monkey FKBP51, to 2.8 A, by using multiwavelength anomalous dispersion phasing. FKBP51 is composed of three domains: two consecutive FKBP domains and a three-unit repeat of the TPR (tetratricopeptide repeat) domain. This structure of a multi-FKBP domain protein clarifies the arrangement of these domains and their possible interactions with other proteins. The two FKBP domains differ by an insertion in the second that affects the formation of the progesterone receptor complex.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1KT1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saimiri_boliviensis Saimiri boliviensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KT1 OCA].
 
==Reference==
Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes., Sinars CR, Cheung-Flynn J, Rimerman RA, Scammell JG, Smith DF, Clardy J, Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):868-73. Epub 2003 Jan 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12538866 12538866]
[[Category: Peptidylprolyl isomerase]]
[[Category: Saimiri boliviensis]]
[[Category: Saimiri boliviensis]]
[[Category: Single protein]]
[[Category: Cheung-Flynn J]]
[[Category: Cheung-Flynn, J.]]
[[Category: Clardy JC]]
[[Category: Clardy, J C.]]
[[Category: Rimerman RA]]
[[Category: Rimerman, R A.]]
[[Category: Scammell JG]]
[[Category: Scammell, J G.]]
[[Category: Sinars CR]]
[[Category: Sinars, C R.]]
[[Category: Smith DF]]
[[Category: Smith, D F.]]
[[Category: SO4]]
[[Category: fkbp-like ppiase]]
[[Category: tpr repeat]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:21:46 2008''

Latest revision as of 07:27, 14 February 2024

Structure of the Large FKBP-like Protein, FKBP51, Involved in Steroid Receptor Complexes

1kt1, resolution 2.80Å

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