1Q1C

Crystal structure of N(1-260) of human FKBP52

1Q1C の概要

• エントリーDOI: 10.2210/pdb1q1c/pdb
• 分子名称: FK506-binding protein 4, DIMETHYL SULFOXIDE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: rotamase, tpr repeat, nuclear protein, phosphorylation, isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytosol (By similarity): Q02790
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31818.16

構造登録者

Wu, B.,Li, P.,Lou, Z.,Ding, Y.,Shu, C.,Shen, B.,Rao, Z. (登録日: 2003-07-18, 公開日: 2004-06-22, 最終更新日: 2024-03-13)

主引用文献

Wu, B.,Li, P.,Liu, Y.,Lou, Z.,Ding, Y.,Shu, C.,Ye, S.,Bartlam, M.,Shen, B.,Rao, Z.
3D structure of human FK506-binding protein 52: Implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex
Proc.Natl.Acad.Sci.USA, 101:8348-8353, 2004

PubMed Abstract: 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.

PubMed: 15159550
DOI: 10.1073/pnas.0305969101

実験手法

X-RAY DIFFRACTION (1.9 Å)