3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex.

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.

authors

Wu B,Li P,Liu Y,Lou Z,Ding Y,Shu C,Ye S,Bartlam M,Shen B,Rao Z

doi

10.1073/pnas.0305969101

keywords:

subject

Has Abstract

pub_date

2004-06-01 00:00:00

pages

8348-53

issue

22

eissn

0027-8424

issn

1091-6490

pii

0305969101

journal_volume

101

pub_type

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