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3D Structure of Human FK506-Binding Protein 52: Implications for the Assembly of the Glucocorticoid Receptor/Hsp90/Immunophilin Heterocomplex
Beili Wu, Pengyun Li, Yiwei Liu, Zhiyong Lou, Yi Ding, Cuiling Shu, Sheng Ye, Mark Bartlam, Beifen Shen, Zihe Rao and Timothy A. Springer
Proceedings of the National Academy of Sciences of the United States of America
Vol. 101, No. 22 (Jun. 1, 2004), pp. 8348-8353
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3372190
Page Count: 6
You can always find the topics here!Topics: Proteins, Molecules, Hydrogen bonds, Steroid receptors, Crystals, Data collection, Stereo, Statistical models, Crystal structure, Architecture
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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.
Proceedings of the National Academy of Sciences of the United States of America © 2004 National Academy of Sciences