Structural biology and structure-based inhibitor design of cholera toxin and heat-labile enterotoxin.
Structural biology studies on cholera toxin and the closely related heat-labile enterotoxin from enterotoxigenic Escherichia coli over the past decade have shed light on the mechanism of toxin action at molecular and atomic levels. Also, components of the extracellular protein secretion apparatus that translocate the toxins across the outer membrane are being investigated. At the same time, structure-based design has led to various classes of compounds targeting different toxin sites, including highly potent multivalent inhibitors that block the toxin receptor-binding process.
Fan
Erkang
E
Department of Biochemistry, Biomolecular Structure Center, University of Washington, Box 357742, Seattle WA 98195, USA.
O'Neal
Claire J
CJ
Mitchell
Daniel D
DD
Robien
Mark A
MA
Zhang
Zhongsheng
Z
Pickens
Jason C
JC
Tan
Xiao-Jian
XJ
Korotkov
Konstantin
K
Roach
Claudia
C
Krumm
Brian
B
Verlinde
Christophe L M J
CL
Merritt
Ethan A
EA
Hol
Wim G J
WG
D001427:Bacterial Toxins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D002772:Cholera Toxin / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D004768:Enterotoxins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D013329:Structure-Activity Relationship; D014734:Vibrio cholerae / Q000378:metabolism*
D001427:Bacterial Toxins; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D002772:Cholera Toxin; C027538:heat-labile enterotoxin, E coli