1KT1

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

1KT1 の概要

• エントリーDOI: 10.2210/pdb1kt1/pdb
• 関連するPDBエントリー: 1kt0
• 分子名称: FK506-binding protein FKBP51, SULFATE ION (3 entities in total)
• 機能のキーワード: fkbp-like ppiase, tpr repeats, isomerase
• 由来する生物種: Saimiri boliviensis (Bolivian squirrel monkey)
• 細胞内の位置: Cytoplasm: Q9XSH5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51443.32

構造登録者

Sinars, C.R.,Cheung-Flynn, J.,Rimerman, R.A.,Scammell, J.G.,Smith, D.F.,Clardy, J.C. (登録日: 2002-01-14, 公開日: 2003-02-04, 最終更新日: 2024-02-14)

主引用文献

Sinars, C.R.,Cheung-Flynn, J.,Rimerman, R.A.,Scammell, J.G.,Smith, D.F.,Clardy, J.C.
STRUCTURE OF THE LARGE FK506-BINDING PROTEIN FKBP51, AN HSP90-BINDING PROTEIN AND A COMPONENT OF STEROID RECEPTOR COMPLEXES
Proc.Natl.Acad.Sci.USA, 100:868-873, 2003

PubMed Abstract: 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.

PubMed: 12538866
DOI: 10.1073/pnas.0231020100

実験手法

X-RAY DIFFRACTION (2.8 Å)