title: A new model of the tautomycin-PP1 complex that is not analogous to the corresponding okadaic acid structure.
abstract: A revised model of PP1-tautomycin (TM) complex suggests that this toxin does not bind in a conformation analogous to its structural cousin okadaic acid (OA), as has been assumed, but instead more resembles the mode of binding adopted by calyculin. This model rationalizes the unexpected potency of a truncated TM analogue lacking the bicyclic ketal common to TM and OA.
authors.affiliation: Department of Chemistry, University of California at Irvine, Irvine, CA 92697, USA.
authors.forename: David A
authors.initials: DA
authors.lastname: Colby
authors.forename: Wen
authors.initials: W
authors.lastname: Liu
authors.forename: James E
authors.initials: JE
authors.lastname: Sheppeck
authors.forename: Hsien Bin
authors.initials: HB
authors.lastname: Huang
authors.forename: Angus C
authors.initials: AC
authors.lastname: Nairn
authors.forename: A Richard
authors.initials: AR
authors.lastname: Chamberlin
mesh_terms: D004791:Enzyme Inhibitors / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D019319:Okadaic Acid / Q000737:chemistry*; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D011714:Pyrans / Q000737:chemistry*; D013141:Spiro Compounds / Q000737:chemistry*
chemical_list: D004791:Enzyme Inhibitors; D011714:Pyrans; D013141:Spiro Compounds; C053079:tautomycin; D019319:Okadaic Acid; D010749:Phosphoprotein Phosphatases