Human FKBP52

spinqualitylabelsall models Human FKBP52 N-terminal complex with ethylene glycol and DMSO (PDB code 1q1c) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Crystal structure of N-terminus of human FKBP52 (1q1c) (see also FK506 binding protein) Publication Abstract from PubMed 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. 3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex., Wu B, Li P, Liu Y, Lou Z, Ding Y, Shu C, Ye S, Bartlam M, Shen B, Rao Z, Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8348-53. Epub 2004 May 24. PMID:15159550 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. The 3D structures of several FKBP family members from various species are solved, most of them comprise 1-2 FK domains (e.g. human FKBP52), while wFKBP73 (e.g. 3jym) has 3 FK domains which is characteristic to plants. A sequence-based structure comparison between each of the 3 FK domains of wFKBP73 (3jym) and the 2 FK domains of hFKBP52 (1q1c) was performed. All 3 FK domains of wFKBP73 adopt a typical FK fold exhibiting significant diversity when superimposed. They are arranged in a linear manner in space as observed in the 2 FK domains of hFKBP52. While the 2 FK domains of hFKBP52 are in the same orientation, the orientation between any 2 consecutive wFK73 domains is different than that between the two FK domains of hFKBP52. Superposition of the wFK73_1 (in blueviolet) and wFK73_2 (in cyan) domains (3jym) on hFK52_1 (in yellow) and hFK52_2 (in blue) revealed that while wFK73_2 is perfectly aligned with hFK52_2, N-terminal wFK73_1 does not align with hFK52_1 (yellow). Similarly, superposition of the wFK73_2 and wFK73_3 (in magenta) domains on hFKBP52 revealed that while wFK73_2 is perfectly aligned with hFK52_1 (in yellow), wFK73_3 does not align with hFK52_2. This unique arrangement of wFKBP73 causes that the α-helices of wFKBP73 3 FK domains are exposed on the same surface, while the 2 α-helices of hFK52 are presented on opposite surfaces. About this Structure 1Q1C is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

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Alexander Berchansky, Michal Harel