Colby David A, Liu Wen, Sheppeck James E, Huang Hsien Bin, Nairn Angus C, Chamberlin A Richard
Department of Chemistry, University of California at Irvine, Irvine, CA 92697, USA.
Bioorg Med Chem Lett. 2003 May 5;13(9):1601-5. doi: 10.1016/s0960-894x(03)00106-9.
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.
蛋白磷酸酶1（PP1）与 tautomycin（TM）复合物的修正模型表明，这种毒素并非如之前所假设的那样，以类似于其结构类似物冈田酸（OA）的构象结合，而是更类似于花萼海绵诱癌素所采用的结合模式。该模型解释了一种缺少TM和OA共有的双环缩酮的截短TM类似物出人意料的效力。
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