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.
journal_name
Proc Natl Acad Sci U S Aauthors
Wu B,Li P,Liu Y,Lou Z,Ding Y,Shu C,Ye S,Bartlam M,Shen B,Rao Zdoi
10.1073/pnas.0305969101keywords:
subject
Has Abstractpub_date
2004-06-01 00:00:00pages
8348-53issue
22eissn
0027-8424issn
1091-6490pii
0305969101journal_volume
101pub_type
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