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10.1016/j.jmb.2014.01.011 http://scihub22266oqcxt.onion/10.1016/j.jmb.2014.01.011 C4041121!4041121!24522230     free     free     free 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 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Mol+Biol 2014 ; 426 (8): 1799-811 Nephropedia Template TP {{tp|p=24522230|t=2014. Immunoglobulin G1 Fc domain motions: implications for Fc engineering |pdf=|usr=}}{{24522230}} gab.com Text Immunoglobulin G1 Fc domain motions: implications for Fc engineering JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=24522230 #FOAvip The fragment crystallizable (Fc) region links the key pathogen identification and destruction properties of immunoglobulin G(IgG). Pathogen opsonization positions Fcs to activate pro-inflammatory Fc? receptors (Fc?Rs) on immune cells. The cellular response and committal to a damaging, though protective, immune response is tightly controlled at multiple levels. Control mechanisms are diverse and in many cases unclear, but one frequently suggested contribution originates in Fc? receptor affinity being modulated through shifts in Fc conformational sampling. Here we report a previously unseen IgG1 Fc conformation. This observation motivated an extensive molecular dynamics (MD) investigation of polypeptide and glycan motions that revealed greater amplitude of motion for the N-terminal C?2 domains and N-glycan than previously observed. Residues in the C?2/C?3 interface and disulphide-bonded hinge were identified as influencing the C?2 motion. Our results are consistent with a model of Fc that is structurally dynamic. Conformational states that are competent to bind immune-stimulating Fc?Rs interconverted with Fc conformations distinct from those observed in Fc?R complexes, which may represent a transient, nonbinding population. Twit Text FOAVip Immunoglobulin G1 Fc domain motions: implications for Fc engineering ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=24522230 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24522230 #FOAvip English Wikipedia <ref>{{Cite pmid|24522230}}</ref> Immunoglobulin G1 Fc domain motions: implications for Fc engineering #MMPMID24522230 Frank M; Walker RC; Lanzilotta WN; Prestegard JH; Barb AW J Mol Biol 2014[Apr]; 426 (8): 1799-811 PMID24522230show ga The fragment crystallizable (Fc) region links the key pathogen identification and destruction properties of immunoglobulin G(IgG). Pathogen opsonization positions Fcs to activate pro-inflammatory Fc? receptors (Fc?Rs) on immune cells. The cellular response and committal to a damaging, though protective, immune response is tightly controlled at multiple levels. Control mechanisms are diverse and in many cases unclear, but one frequently suggested contribution originates in Fc? receptor affinity being modulated through shifts in Fc conformational sampling. Here we report a previously unseen IgG1 Fc conformation. This observation motivated an extensive molecular dynamics (MD) investigation of polypeptide and glycan motions that revealed greater amplitude of motion for the N-terminal C?2 domains and N-glycan than previously observed. Residues in the C?2/C?3 interface and disulphide-bonded hinge were identified as influencing the C?2 motion. Our results are consistent with a model of Fc that is structurally dynamic. Conformational states that are competent to bind immune-stimulating Fc?Rs interconverted with Fc conformations distinct from those observed in Fc?R complexes, which may represent a transient, nonbinding population. äImmunoglobulin G1 Fc domain motions: implications for Fc engineering (epmc).pdf DeepDyve Pubget Overpricing