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10.1038/srep44388 http://scihub22266oqcxt.onion/10.1038/srep44388 C5347425!5347425 !28287617     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28287617 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Sci+Rep 2017 ; 7 (ä): 44388 Nephropedia Template TP {{tp|p=28287617 |t=2017. Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly |pdf=|usr=}}{{28287617 }} gab.com Text Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28287617 #FOAvip Domain swapping is the process by which identical proteins exchange reciprocal segments to generate dimers. Here we introduce induced domain swapping (INDOS) as a mechanism for regulating protein function. INDOS employs a modular design consisting of the fusion of two proteins: a recognition protein that binds a triggering molecule, and a target protein that undergoes a domain swap in response to binding of the triggering ligand. The recognition protein (FK506 binding protein) is inserted into functionally-inactivated point mutants of two target proteins (staphylococcal nuclease and ribose binding protein). Binding of FK506 to the FKBP domain causes the target domain to first unfold, then refold via domain swap. The inactivating mutations become 'swapped out' in the dimer, increasing nuclease and ribose binding activities by 100-fold and 15-fold, respectively, restoring them to near wild-type values. INDOS is intended to convert an arbitrary protein into a functional switch, and is the first example of rational design in which a small molecule is used to trigger protein domain swapping and subsequent activation of biological function. Twit Text FOAVip Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28287617 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28287617 #FOAvip English Wikipedia <ref>{{Cite pmid|28287617 }}</ref> Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly #MMPMID28287617 Karchin JM ; Ha JH ; Namitz KE ; Cosgrove MS ; Loh SN Sci Rep 2017[Mar]; 7 (ä): 44388 PMID28287617 show ga Domain swapping is the process by which identical proteins exchange reciprocal segments to generate dimers. Here we introduce induced domain swapping (INDOS) as a mechanism for regulating protein function. INDOS employs a modular design consisting of the fusion of two proteins: a recognition protein that binds a triggering molecule, and a target protein that undergoes a domain swap in response to binding of the triggering ligand. The recognition protein (FK506 binding protein) is inserted into functionally-inactivated point mutants of two target proteins (staphylococcal nuclease and ribose binding protein). Binding of FK506 to the FKBP domain causes the target domain to first unfold, then refold via domain swap. The inactivating mutations become 'swapped out' in the dimer, increasing nuclease and ribose binding activities by 100-fold and 15-fold, respectively, restoring them to near wild-type values. INDOS is intended to convert an arbitrary protein into a functional switch, and is the first example of rational design in which a small molecule is used to trigger protein domain swapping and subsequent activation of biological function. |Bacterial Proteins/*chemistry/genetics/metabolism [MESH] |Binding Sites [MESH] |Cloning, Molecular [MESH] |Deoxyribonucleases/*chemistry/genetics/metabolism [MESH] |Escherichia coli/genetics/metabolism [MESH] |Gene Expression [MESH] |Genetic Vectors/chemistry/metabolism [MESH] |Humans [MESH] |Kinetics [MESH] |Models, Molecular [MESH] |Mutation [MESH] |Periplasmic Binding Proteins/*chemistry/genetics/metabolism [MESH] |Protein Binding [MESH] |Protein Conformation, alpha-Helical [MESH] |Protein Conformation, beta-Strand [MESH] |Protein Interaction Domains and Motifs [MESH] |Recombinant Proteins/chemistry/genetics/metabolism [MESH] |Substrate Specificity [MESH] |TOR Serine-Threonine Kinases/*chemistry/genetics/metabolism [MESH] |Tacrolimus/*chemistry/metabolism [MESH] |Thermoanaerobacter/chemistry [MESH]Small Molecule-Induced Domain Swapping as a Mechanism for Controlling (epmc).pdf DeepDyve Pubget Overpricing