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10.1021/bi9007808 http://scihub22266oqcxt.onion/10.1021/bi9007808 19653656!ä!19653656 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       Biochemistry 2009 ; 48 (36): 8758-63 Nephropedia Template TP {{tp|p=19653656|t=2009. Ion-blocking sites of the Kir2 1 channel revealed by multiscale modeling |pdf=|usr=}}{{19653656}} gab.com Text Ion-blocking sites of the Kir2 1 channel revealed by multiscale modeling JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=19653656 #FOAvip The Kir2.1 potassium channel owes its inward-rectifying behavior to blocking by multivalent ions, e.g., magnesium and spermine, which access the channel from the cytoplasm and are thought to bind within the pore. To investigate the pathway followed by these ions from the cytoplasm through the pore, we have used multiscale modeling (via continuum electrostatics calculations, docking, and molecular dynamics simulations) to identify possible binding sites en route. On its way to eventually binding in the cavity, magnesium interacts extensively with Glu299, which lines the pore in the center of the intracellular domain. Interaction sites for spermine are formed by Asp255, Glu299, and Glu224. Entropic factors seem to favor interactions of spermine within the center of the cytoplasmic domain. Twit Text FOAVip Ion-blocking sites of the Kir2 1 channel revealed by multiscale modeling ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=19653656 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19653656 #FOAvip English Wikipedia <ref>{{Cite pmid|19653656}}</ref> Ion-blocking sites of the Kir2 1 channel revealed by multiscale modeling #MMPMID19653656 Tai K; Stansfeld PJ; Sansom MS Biochemistry 2009[Sep]; 48 (36): 8758-63 PMID19653656show ga The Kir2.1 potassium channel owes its inward-rectifying behavior to blocking by multivalent ions, e.g., magnesium and spermine, which access the channel from the cytoplasm and are thought to bind within the pore. To investigate the pathway followed by these ions from the cytoplasm through the pore, we have used multiscale modeling (via continuum electrostatics calculations, docking, and molecular dynamics simulations) to identify possible binding sites en route. On its way to eventually binding in the cavity, magnesium interacts extensively with Glu299, which lines the pore in the center of the intracellular domain. Interaction sites for spermine are formed by Asp255, Glu299, and Glu224. Entropic factors seem to favor interactions of spermine within the center of the cytoplasmic domain. |*Models, Molecular[MESH] |Animals[MESH] |Computer Simulation[MESH] |G Protein-Coupled Inwardly-Rectifying Potassium Channels/antagonists & inhibitors/chemistry/genetics[MESH] |Humans[MESH] |Ion Channel Gating/genetics[MESH] |Magnesium/chemistry[MESH] |Mice[MESH] |Potassium Channel Blockers/*chemistry[MESH] |Potassium Channels, Inwardly Rectifying/*antagonists & inhibitors/*chemistry/genetics[MESH] |Protein Structure, Tertiary/genetics[MESH] |Spermidine/chemistry[MESH] |Spermine/chemistry[MESH] |Static Electricity[MESH] |Structural Homology, Protein[MESH]Ion-blocking sites of the Kir2 1 channel revealed by multiscale modeli(epmc).pdf DeepDyve Pubget Overpricing