1kt0

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|PDB= 1kt0 |SIZE=350|CAPTION= <scene name='initialview01'>1kt0</scene>, resolution 2.70&Aring;
|PDB= 1kt0 |SIZE=350|CAPTION= <scene name='initialview01'>1kt0</scene>, resolution 2.70&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|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]
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|ACTIVITY= <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>
|GENE= FKBP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= FKBP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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|RELATEDENTRY=[[1kt1|1KT1]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kt0 OCA], [http://www.ebi.ac.uk/pdbsum/1kt0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kt0 RCSB]</span>
}}
}}
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[[Category: Sinars, C R.]]
[[Category: Sinars, C R.]]
[[Category: Smith, D F.]]
[[Category: Smith, D F.]]
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[[Category: SO4]]
 
[[Category: fkbp-like ppiase]]
[[Category: fkbp-like ppiase]]
[[Category: tpr repeat]]
[[Category: tpr repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:21:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:53:10 2008''

Revision as of 18:53, 30 March 2008


PDB ID 1kt0

Drag the structure with the mouse to rotate
, resolution 2.70Å
Ligands:
Gene: FKBP5 (Homo sapiens)
Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8
Related: 1KT1


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Contents

Overview

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.

Disease

Known disease associated with this structure: Major depressive disorder and accelerated response to antidepressant drug treatment OMIM:[602623]

About this Structure

1KT0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from 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:12538866

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