Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

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
Stable URL: http://www.jstor.org/stable/3372190
Page Count: 6
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
3D Structure of Human FK506-Binding Protein 52: Implications for the Assembly of the Glucocorticoid Receptor/Hsp90/Immunophilin Heterocomplex
Preview not available

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.

Page Thumbnails

  • Thumbnail: Page 
[8348]
    [8348]
  • Thumbnail: Page 
8349
    8349
  • Thumbnail: Page 
8350
    8350
  • Thumbnail: Page 
8351
    8351
  • Thumbnail: Page 
8352
    8352
  • Thumbnail: Page 
8353
    8353