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10.1073/pnas.1418402111 http://scihub22266oqcxt.onion/10.1073/pnas.1418402111 C4217441!4217441!25319261     free     free     free       Proc+Natl+Acad+Sci+U+S+A 2014 ; 111 (43): E4623-31 Nephropedia Template TP {{tp|p=25319261|t=2014. Dynamic architecture of a protein kinase |pdf=|usr=}}{{25319261}} gab.com Text Dynamic architecture of a protein kinase JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25319261 #FOAvip Protein kinases represent a critically important family of regulatory enzymes. Their activity can be altered by mutations and binding events distant from the active site. To understand the nature of these long-distance effects, we used microsecond-timescale molecular dynamic simulation to subdivide a prototypical kinase, protein kinase A, into contiguous communities that exhibit internally correlated motions. Surprisingly, most of these unconventional structural entities were centered around known protein kinase functions. We thus propose a new framework for analysis of protein kinase structure and function that differs from traditional representations based simply on sequence motifs and secondary structure elements. These results extend our view on the dynamic nature of protein kinases and open a door to understanding of allosteric signaling in these enzymes. Twit Text FOAVip Dynamic architecture of a protein kinase ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25319261 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25319261 #FOAvip English Wikipedia <ref>{{Cite pmid|25319261}}</ref> Dynamic architecture of a protein kinase #MMPMID25319261 McClendon CL; Kornev AP; Gilson MK; Taylor SS Proc Natl Acad Sci U S A 2014[Oct]; 111 (43): E4623-31 PMID25319261show ga Protein kinases represent a critically important family of regulatory enzymes. Their activity can be altered by mutations and binding events distant from the active site. To understand the nature of these long-distance effects, we used microsecond-timescale molecular dynamic simulation to subdivide a prototypical kinase, protein kinase A, into contiguous communities that exhibit internally correlated motions. Surprisingly, most of these unconventional structural entities were centered around known protein kinase functions. We thus propose a new framework for analysis of protein kinase structure and function that differs from traditional representations based simply on sequence motifs and secondary structure elements. These results extend our view on the dynamic nature of protein kinases and open a door to understanding of allosteric signaling in these enzymes. äDynamic architecture of a protein kinase (epmc).pdf DeepDyve Pubget Overpricing