Author: So Young Kim; Weihua Jin; Amika Sood; David W. Montgomery; Oliver C. Grant; Mark M. Fuster; Li Fu; Jonathan S. Dordick; Robert J. Woods; Fuming Zhang; Robert J. Linhardt
Title: Glycosaminoglycan binding motif at S1/S2 proteolytic cleavage site on spike glycoprotein may facilitate novel coronavirus (SARS-CoV-2) host cell entry Document date: 2020_4_15
ID: fs8dn7ir_43
Snippet: The 3D coordinates for the SGP trimer (NCBI reference sequence YP_009724390.1) were downloaded from the SWISS-MODEL homology modeling server [34] . The selected model was generated with the Cryo-EM structure PDB ID 6VSB as a template, which has a 99.26% sequence identity and 95% coverage for amino acids 27 to 1146. The template and resulting model is the "prefusion" structure with one of the three receptor binding domains (Chain A) in the "up" or.....
Document: The 3D coordinates for the SGP trimer (NCBI reference sequence YP_009724390.1) were downloaded from the SWISS-MODEL homology modeling server [34] . The selected model was generated with the Cryo-EM structure PDB ID 6VSB as a template, which has a 99.26% sequence identity and 95% coverage for amino acids 27 to 1146. The template and resulting model is the "prefusion" structure with one of the three receptor binding domains (Chain A) in the "up" or "open" conformation [30] . Cryo-EM studies have revealed that the SARS-CoV-2 SGP trimer exists in two conformational states in approximately equal abundance [35] . In one state, all SGP monomers have their hACE2-binding domain closed, and in the other, one monomer has its hACE2-binding domain open, where it is positioned away from the interior of the protein.
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