Syntheses of photolabile novobiocin analogues.
Novobiocin was recently shown to inhibit Hsp90 through a previously unrecognized C-terminal ATP binding site. Although the N-terminal region of Hsp90 has been solved by X-ray crystallography, the C-terminal region has not. In an effort to elucidate the C-terminal binding site of Hsp90, four photolabile analogues of novobiocin were prepared.
Shen
Gang
G
Department of Medicinal Chemistry and The Center for Protein Structure and Function, The University of Kansas, 1251 Wescoe Hall Drive, Malott Hall 4070, Lawrence, KS 66045-7562, USA.
Yu
Xiao Ming
XM
Blagg
Brian S J
BS
D001665:Binding Sites / Q000502:physiology; D008029:Lighting / Q000009:adverse effects; D009675:Novobiocin / Q000031:analogs & derivatives* / Q000138:chemical synthesis* / Q000378:metabolism
D009675:Novobiocin