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10.1016/j.jmb.2012.02.012 http://scihub22266oqcxt.onion/10.1016/j.jmb.2012.02.012 C4603570!4603570 !22366544     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=22366544 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 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\22366544 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Mol+Biol 2012 ; 418 (1-2 ): 103-16 Nephropedia Template TP {{tp|p=22366544 |t=2012. Structural basis for profilin-mediated actin nucleotide exchange |pdf=|usr=}}{{22366544 }} gab.com Text Structural basis for profilin-mediated actin nucleotide exchange JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=22366544 #FOAvip Actin is a ubiquitous eukaryotic protein that is responsible for cellular scaffolding, motility, and division. The ability of actin to form a helical filament is the driving force behind these cellular activities. Formation of a filament depends on the successful exchange of actin's ADP for ATP. Mammalian profilin is a small actin binding protein that catalyzes the exchange of nucleotide and facilitates the addition of an actin monomer to a growing filament. Here, crystal structures of profilin-actin have been determined to show an actively exchanging ATP. Structural analysis shows how the binding of profilin to the barbed end of actin causes a rotation of the small domain relative to the large domain. This conformational change is propagated to the ATP site and causes a shift in nucleotide loops, which in turn causes a repositioning of Ca(2+) to its canonical position as the cleft closes around ATP. Reversal of the solvent exposure of Trp356 is also involved in cleft closure. In addition, secondary calcium binding sites were identified. Twit Text FOAVip Structural basis for profilin-mediated actin nucleotide exchange ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=22366544 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=22366544 #FOAvip English Wikipedia <ref>{{Cite pmid|22366544 }}</ref> Structural basis for profilin-mediated actin nucleotide exchange #MMPMID22366544 Porta JC ; Borgstahl GE J Mol Biol 2012[Apr]; 418 (1-2 ): 103-16 PMID22366544 show ga Actin is a ubiquitous eukaryotic protein that is responsible for cellular scaffolding, motility, and division. The ability of actin to form a helical filament is the driving force behind these cellular activities. Formation of a filament depends on the successful exchange of actin's ADP for ATP. Mammalian profilin is a small actin binding protein that catalyzes the exchange of nucleotide and facilitates the addition of an actin monomer to a growing filament. Here, crystal structures of profilin-actin have been determined to show an actively exchanging ATP. Structural analysis shows how the binding of profilin to the barbed end of actin causes a rotation of the small domain relative to the large domain. This conformational change is propagated to the ATP site and causes a shift in nucleotide loops, which in turn causes a repositioning of Ca(2+) to its canonical position as the cleft closes around ATP. Reversal of the solvent exposure of Trp356 is also involved in cleft closure. In addition, secondary calcium binding sites were identified. |Actins/*chemistry/metabolism [MESH] |Adenosine Triphosphate/*chemistry/metabolism [MESH] |Animals [MESH] |Binding Sites [MESH] |Calcium/chemistry/metabolism [MESH] |Cattle [MESH] |Profilins/*chemistry/metabolism [MESH]Structural basis for profilin-mediated actin nucleotide exchange (epmc).pdf DeepDyve Pubget Overpricing