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| | <StructureSection load='1kt1' size='340' side='right'caption='[[1kt1]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1kt1' size='340' side='right'caption='[[1kt1]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kt1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bolivian_squirrel_monkey Bolivian squirrel monkey]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KT1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kt1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bolivian_squirrel_monkey Bolivian squirrel monkey]. 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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kt0|1kt0]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kt0|1kt0]]</div></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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://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=1kt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kt1 OCA], [http://pdbe.org/1kt1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kt1 RCSB], [http://www.ebi.ac.uk/pdbsum/1kt1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kt1 ProSAT]</span></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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [[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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[FK506 binding protein|FK506 binding protein]] | + | *[[FKBP 3D structures|FKBP 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[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.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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:12538866[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Denny WB, Valentine DL, Reynolds PD, Smith DF, Scammell JG. Squirrel monkey immunophilin FKBP51 is a potent inhibitor of glucocorticoid receptor binding. Endocrinology. 2000 Nov;141(11):4107-13. PMID:11089542 doi:http://dx.doi.org/10.1210/endo.141.11.7785
- ↑ Sinars CR, Cheung-Flynn J, Rimerman RA, Scammell JG, Smith DF, Clardy J. Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes. Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):868-73. Epub 2003 Jan 21. PMID:12538866 doi:10.1073/pnas.0231020100
- ↑ Sinars CR, Cheung-Flynn J, Rimerman RA, Scammell JG, Smith DF, Clardy J. Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes. Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):868-73. Epub 2003 Jan 21. PMID:12538866 doi:10.1073/pnas.0231020100
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