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10.1038/srep22298 http://scihub22266oqcxt.onion/10.1038/srep22298 C4773988!4773988!26931396     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2016 ; 6 (ä): ä Nephropedia Template TP {{tp|p=26931396|t=2016. Structure-based Inhibitor Design for the Intrinsically Disordered Protein c-Myc |pdf=|usr=}}{{26931396}} gab.com Text Structure-based Inhibitor Design for the Intrinsically Disordered Protein c-Myc JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26931396 #FOAvip Intrinsically disordered proteins (IDPs) are associated with various diseases and have been proposed as promising drug targets. However, conventional structure-based approaches cannot be applied directly to IDPs, due to their lack of ordered structures. Here, we describe a novel computational approach to virtually screen for compounds that can simultaneously bind to different IDP conformations. The test system used c-Myc, an oncoprotein containing a disordered basic helix-loop-helix-leucine zipper (bHLH-LZ) domain that adopts a helical conformation upon binding to Myc-associated factor X (Max). For the virtual screen, we used three binding pockets in representative conformations of c-Myc370?409, which is part of the disordered bHLH-LZ domain. Seven compounds were found to directly bind c-Myc370?409in vitro, and four inhibited the growth of the c-Myc-overexpressing cells by affecting cell cycle progression. Our approach of IDP conformation sampling, binding site identification, and virtual screening for compounds that can bind to multiple conformations provides a useful strategy for structure-based drug discovery targeting IDPs. Twit Text FOAVip Structure-based Inhibitor Design for the Intrinsically Disordered Protein c-Myc ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26931396 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26931396 #FOAvip English Wikipedia <ref>{{Cite pmid|26931396}}</ref> Structure-based Inhibitor Design for the Intrinsically Disordered Protein c-Myc #MMPMID26931396 Yu C; Niu X; Jin F; Liu Z; Jin C; Lai L Sci Rep 2016[]; 6 (ä): ä PMID26931396show ga Intrinsically disordered proteins (IDPs) are associated with various diseases and have been proposed as promising drug targets. However, conventional structure-based approaches cannot be applied directly to IDPs, due to their lack of ordered structures. Here, we describe a novel computational approach to virtually screen for compounds that can simultaneously bind to different IDP conformations. The test system used c-Myc, an oncoprotein containing a disordered basic helix-loop-helix-leucine zipper (bHLH-LZ) domain that adopts a helical conformation upon binding to Myc-associated factor X (Max). For the virtual screen, we used three binding pockets in representative conformations of c-Myc370?409, which is part of the disordered bHLH-LZ domain. Seven compounds were found to directly bind c-Myc370?409in vitro, and four inhibited the growth of the c-Myc-overexpressing cells by affecting cell cycle progression. Our approach of IDP conformation sampling, binding site identification, and virtual screening for compounds that can bind to multiple conformations provides a useful strategy for structure-based drug discovery targeting IDPs. äStructure-based Inhibitor Design for the Intrinsically Disordered Prot(epmc).pdf DeepDyve Pubget Overpricing