1P5Q

Crystal Structure of FKBP52 C-terminal Domain

Summary for 1P5Q

• Entry DOI: 10.2210/pdb1p5q/pdb
• Descriptor: FK506-binding protein 4, SULFATE ION (3 entities in total)
• Functional Keywords: isomerase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol (By similarity): Q02790
• Total number of polymer chains: 3
• Total formula weight: 116172.09

Authors

Wu, B.,Li, P.,Lou, Z.,Shu, C.,Ding, Y.,Shen, B.,Rao, Z. (deposition date: 2003-04-28, release date: 2004-06-22, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)