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10.1016/j.bpj.2021.01.037 http://scihub22266oqcxt.onion/10.1016/j.bpj.2021.01.037 33609494!7889469!33609494     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2021 ; 120 (6): 983-993 Nephropedia Template TP {{tp|p=33609494|t=2021. A potential interaction between the SARS-CoV-2 spike protein and nicotinic acetylcholine receptors |pdf=|usr=}}{{33609494}} gab.com Text A potential interaction between the SARS-CoV-2 spike protein and nicotinic acetylcholine receptors JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=33609494 #FOAvip Changeux et al. (Changeux et al. C. R. Biol. 343:33-39.) recently suggested that the SARS-CoV-2 spike protein may interact with nicotinic acetylcholine receptors (nAChRs) and that such interactions may be involved in pathology and infectivity. This hypothesis is based on the fact that the SARS-CoV-2 spike protein contains a sequence motif similar to known nAChR antagonists. Here, we use molecular simulations of validated atomically detailed structures of nAChRs and of the spike to investigate the possible binding of the Y674-R685 region of the spike to nAChRs. We examine the binding of the Y674-R685 loop to three nAChRs, namely the human alpha4beta2 and alpha7 subtypes and the muscle-like alphabetagammadelta receptor from Tetronarce californica. Our results predict that Y674-R685 has affinity for nAChRs. The region of the spike responsible for binding contains a PRRA motif, a four-residue insertion not found in other SARS-like coronaviruses. The conformational behavior of the bound Y674-R685 is highly dependent on the receptor subtype; it adopts extended conformations in the alpha4beta2 and alpha7 complexes but is more compact when bound to the muscle-like receptor. In the alpha4beta2 and alphabetagammadelta complexes, the interaction of Y674-R685 with the receptors forces the loop C region to adopt an open conformation, similar to other known nAChR antagonists. In contrast, in the alpha7 complex, Y674-R685 penetrates deeply into the binding pocket in which it forms interactions with the residues lining the aromatic box, namely with TrpB, TyrC1, and TyrC2. Estimates of binding energy suggest that Y674-R685 forms stable complexes with all three nAChR subtypes. Analyses of simulations of the glycosylated spike show that the Y674-R685 region is accessible for binding. We suggest a potential binding orientation of the spike protein with nAChRs, in which they are in a nonparallel arrangement to one another. Twit Text FOAVip A potential interaction between the SARS-CoV-2 spike protein and nicotinic acetylcholine receptors ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=33609494 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33609494 #FOAvip English Wikipedia <ref>{{Cite pmid|33609494}}</ref> A potential interaction between the SARS-CoV-2 spike protein and nicotinic acetylcholine receptors #MMPMID33609494 Oliveira ASF; Ibarra AA; Bermudez I; Casalino L; Gaieb Z; Shoemark DK; Gallagher T; Sessions RB; Amaro RE; Mulholland AJ Biophys J 2021[Mar]; 120 (6): 983-993 PMID33609494show ga Changeux et al. (Changeux et al. C. R. Biol. 343:33-39.) recently suggested that the SARS-CoV-2 spike protein may interact with nicotinic acetylcholine receptors (nAChRs) and that such interactions may be involved in pathology and infectivity. This hypothesis is based on the fact that the SARS-CoV-2 spike protein contains a sequence motif similar to known nAChR antagonists. Here, we use molecular simulations of validated atomically detailed structures of nAChRs and of the spike to investigate the possible binding of the Y674-R685 region of the spike to nAChRs. We examine the binding of the Y674-R685 loop to three nAChRs, namely the human alpha4beta2 and alpha7 subtypes and the muscle-like alphabetagammadelta receptor from Tetronarce californica. Our results predict that Y674-R685 has affinity for nAChRs. The region of the spike responsible for binding contains a PRRA motif, a four-residue insertion not found in other SARS-like coronaviruses. The conformational behavior of the bound Y674-R685 is highly dependent on the receptor subtype; it adopts extended conformations in the alpha4beta2 and alpha7 complexes but is more compact when bound to the muscle-like receptor. In the alpha4beta2 and alphabetagammadelta complexes, the interaction of Y674-R685 with the receptors forces the loop C region to adopt an open conformation, similar to other known nAChR antagonists. In contrast, in the alpha7 complex, Y674-R685 penetrates deeply into the binding pocket in which it forms interactions with the residues lining the aromatic box, namely with TrpB, TyrC1, and TyrC2. Estimates of binding energy suggest that Y674-R685 forms stable complexes with all three nAChR subtypes. Analyses of simulations of the glycosylated spike show that the Y674-R685 region is accessible for binding. We suggest a potential binding orientation of the spike protein with nAChRs, in which they are in a nonparallel arrangement to one another. |Glycosylation[MESH] |Humans[MESH] |Molecular Dynamics Simulation[MESH] |Peptides/chemistry/metabolism[MESH] |Protein Binding[MESH] |Receptors, Nicotinic/chemistry/*metabolism[MESH] |Spike Glycoprotein, Coronavirus/chemistry/*metabolism[MESH]A potential interaction between the SARS-CoV-2 spike protein and nicot(epmc).pdf DeepDyve Pubget Overpricing