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Structure of the human 25 kDa FK506 binding protein complexed with rapamycin

Authors :
Liang, Jun
Hung, Deborah T.
Schreiber, Stuart L.
Clardy, Jon
Source :
Journal of the American Chemical Society. Feb 7, 1996, Vol. 118 Issue 5, p1231, 2 p.
Publication Year :
1996

Abstract

FKBP25 is the third member of the family of binding proteins that has an immunosuppressive function. Its C-terminal domain has been suggested to contain a nuclear localization sequence that can be used as a binding site. X-ray diffraction of the C-terminal domain, which was performed by complexing it with rapamycin, revealed a predominant secondary structure consisting of a curved beta-sheet made from five antiparallel beta strands. Adjacent to the beta sheet is a short turn of alpha-helix which contributes a tryptophan to the binding pocket.

Details

ISSN :
00027863
Volume :
118
Issue :
5
Database :
Gale General OneFile
Journal :
Journal of the American Chemical Society
Publication Type :
Academic Journal
Accession number :
edsgcl.18152823