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10.1021/acs.jpcb.1c00304 http://scihub22266oqcxt.onion/10.1021/acs.jpcb.1c00304 33661628!8279474!33661628     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33661628&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 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Phys+Chem+B 2021 ; 125 (10): 2607-2616 Nephropedia Template TP {{tp|p=33661628|t=2021. Oligomannose N-Glycans 3D Architecture and Its Response to the FcgammaRIIIa Structural Landscape |pdf=|usr=}}{{33661628}} gab.com Text Oligomannose N-Glycans 3D Architecture and Its Response to the FcgammaRIIIa Structural Landscape JO: J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=33661628 #FOAvip Oligomannoses are evolutionarily the oldest class of N-glycans, where the arms of the common pentasaccharide unit, i.e., Manalpha(1-6)-[Manalpha(1-3)]-Manbeta(1-4)-GlcNAcbeta(1-4)-GlcNAcbeta1-Asn, are functionalized exclusively with branched arrangements of mannose (Man) monosaccharide units. In mammalian species oligomannose N-glycans can have up to 9 Man; meanwhile structures can grow to over 200 units in yeast mannan. The highly dynamic nature, branching complexity, and 3D structure of oligomannoses have been recently highlighted for their roles in immune escape and infectivity of enveloped viruses, such as HIV-1 and SARS-CoV2. The architectural features that allow these N-glycans to perform their functions are yet unclear, due to their intrinsically disordered nature that hinders their structural characterization. In this work we will discuss the results of over 54 mus of cumulative sampling by molecular dynamics (MD) simulations of differently processed, free (not protein-linked) oligomannose N-glycans common in vertebrates. We then discuss the effects of a protein surface on their structural equilibria based on over 4 mus cumulative MD sampling of the fully glycosylated CD16a Fc gamma receptor (FcgammaRIIIa), where the type of glycosylation is known to modulate its binding affinity for IgG1s, regulating the antibody-dependent cellular cytotoxicity (ADCC). Our results show that the protein's structural constraints shift the oligomannoses conformational ensemble to promote conformers that satisfy the steric requirements and hydrogen bonding networks demanded by the protein's surface landscape. More importantly, we find that the protein does not actively distort the N-glycans into structures not populated in the unlinked forms in solution. Ultimately, the highly populated conformations of the Man5 linked glycans support experimental evidence of high levels of hybrid complex forms at N45 and show a specific presentation of the arms at N162, which may be involved in mediating binding affinity to the IgG1 Fc. Twit Text FOAVip Oligomannose N-Glycans 3D Architecture and Its Response to the FcgammaRIIIa Structural Landscape ????J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=33661628 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33661628 #FOAvip English Wikipedia <ref>{{Cite pmid|33661628}}</ref> Oligomannose N-Glycans 3D Architecture and Its Response to the FcgammaRIIIa Structural Landscape #MMPMID33661628 Fogarty CA; Fadda E J Phys Chem B 2021[Mar]; 125 (10): 2607-2616 PMID33661628show ga Oligomannoses are evolutionarily the oldest class of N-glycans, where the arms of the common pentasaccharide unit, i.e., Manalpha(1-6)-[Manalpha(1-3)]-Manbeta(1-4)-GlcNAcbeta(1-4)-GlcNAcbeta1-Asn, are functionalized exclusively with branched arrangements of mannose (Man) monosaccharide units. In mammalian species oligomannose N-glycans can have up to 9 Man; meanwhile structures can grow to over 200 units in yeast mannan. The highly dynamic nature, branching complexity, and 3D structure of oligomannoses have been recently highlighted for their roles in immune escape and infectivity of enveloped viruses, such as HIV-1 and SARS-CoV2. The architectural features that allow these N-glycans to perform their functions are yet unclear, due to their intrinsically disordered nature that hinders their structural characterization. In this work we will discuss the results of over 54 mus of cumulative sampling by molecular dynamics (MD) simulations of differently processed, free (not protein-linked) oligomannose N-glycans common in vertebrates. We then discuss the effects of a protein surface on their structural equilibria based on over 4 mus cumulative MD sampling of the fully glycosylated CD16a Fc gamma receptor (FcgammaRIIIa), where the type of glycosylation is known to modulate its binding affinity for IgG1s, regulating the antibody-dependent cellular cytotoxicity (ADCC). Our results show that the protein's structural constraints shift the oligomannoses conformational ensemble to promote conformers that satisfy the steric requirements and hydrogen bonding networks demanded by the protein's surface landscape. More importantly, we find that the protein does not actively distort the N-glycans into structures not populated in the unlinked forms in solution. Ultimately, the highly populated conformations of the Man5 linked glycans support experimental evidence of high levels of hybrid complex forms at N45 and show a specific presentation of the arms at N162, which may be involved in mediating binding affinity to the IgG1 Fc. |*COVID-19[MESH] |*Receptors, IgG[MESH] |Animals[MESH] |Humans[MESH] |Polysaccharides[MESH] |RNA, Viral[MESH]Oligomannose N-Glycans 3D Architecture and Its Response to the Fcgamma(epmc).pdf DeepDyve Pubget Overpricing