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10.1007/s12551-015-0171-9 http://scihub22266oqcxt.onion/10.1007/s12551-015-0171-9 C4610412!4610412!26495045     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26495045.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biophys+Rev 2015 ; 7 (2): 239-49 Nephropedia Template TP {{tp|p=26495045|t=2015. Investigating dynamic interdomain allostery in Pin1 |pdf=|usr=}}{{26495045}} gab.com Text Investigating dynamic interdomain allostery in Pin1 JO: Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=26495045 #FOAvip Signaling proteins often sequester complementary functional sites in separate domains. How do the different domains communicate with one another? An attractive system to address this question is the mitotic regulator, human Pin1 (Lu et al., Nature 380:544?547, 1996). Pin-1 consists of two mutually tethered domains: a WW domain for substrate binding and a catalytic domain for peptidyl-prolyl isomerase (PPIase) activity. Pin1 accelerates the cis?trans isomerization of phospho-Ser/Thr-Pro (pS/T-P) motifs within proteins regulating the cell cycle and neuronal development. The early X-ray (Ranganathan et al., Cell 89:875?886, 1997; Verdecia et al., Nat Struct Biol 7:639?643, 2000) and solution NMR studies (Bayer et al., J Biol Chem 278:26183?26193, 2003; Jacobs et al., J Biol Chem 278:26174?26182, 2003) of Pin1 indicated inter- and intradomain motions. We have explored how such motions might affect interdomain communication, using NMR. Our accumulated results indicate substrate binding to Pin1 WW domain changes the intra/interdomain mobility, thereby altering substrate activity in the distal PPIase domain catalytic site. Thus, Pin1 shows evidence of dynamic allostery, in the sense of Cooper and Dryden (Eur J Biochem 11:103?109, 1984). We highlight our results supporting this conclusion and summarize them via a simple speculative model of conformational selection. Twit Text FOAVip Investigating dynamic interdomain allostery in Pin1 ????Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=26495045 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26495045 #FOAvip English Wikipedia <ref>{{Cite pmid|26495045}}</ref> Investigating dynamic interdomain allostery in Pin1 #MMPMID26495045 Peng JW Biophys Rev 2015[Jun]; 7 (2): 239-49 PMID26495045show ga Signaling proteins often sequester complementary functional sites in separate domains. How do the different domains communicate with one another? An attractive system to address this question is the mitotic regulator, human Pin1 (Lu et al., Nature 380:544?547, 1996). Pin-1 consists of two mutually tethered domains: a WW domain for substrate binding and a catalytic domain for peptidyl-prolyl isomerase (PPIase) activity. Pin1 accelerates the cis?trans isomerization of phospho-Ser/Thr-Pro (pS/T-P) motifs within proteins regulating the cell cycle and neuronal development. The early X-ray (Ranganathan et al., Cell 89:875?886, 1997; Verdecia et al., Nat Struct Biol 7:639?643, 2000) and solution NMR studies (Bayer et al., J Biol Chem 278:26183?26193, 2003; Jacobs et al., J Biol Chem 278:26174?26182, 2003) of Pin1 indicated inter- and intradomain motions. We have explored how such motions might affect interdomain communication, using NMR. Our accumulated results indicate substrate binding to Pin1 WW domain changes the intra/interdomain mobility, thereby altering substrate activity in the distal PPIase domain catalytic site. Thus, Pin1 shows evidence of dynamic allostery, in the sense of Cooper and Dryden (Eur J Biochem 11:103?109, 1984). We highlight our results supporting this conclusion and summarize them via a simple speculative model of conformational selection. äInvestigating dynamic interdomain allostery in Pin1 (epmc).pdf DeepDyve Pubget Overpricing