Author: Mushtaq Hussain; Nusrat Jabeen; Anusha Amanullah; Ayesha Ashraf Baig; Basma Aziz; Sanya Shabbir; Fozia Raza
Title: Structural Basis of SARS-CoV-2 Spike Protein Priming by TMPRSS2 Document date: 2020_4_22
ID: 34ljq0qt_12
Snippet: Full length molecular models of TMRPSS2 has considerable structural homology with the template molecule (PDB: 1Z8G), where the deviation between the Cα back bone of model and template was found as 0.33Å ( Figure 1E ;F). All three domains, LDL-receptor class A, SRCR and peptidase S1, formed distinct structural units in the molecular model. N-terminal region and LDL-receptor class A of TMPRSS2 were found more or less unstructured ( Figure 1G ;H)......
Document: Full length molecular models of TMRPSS2 has considerable structural homology with the template molecule (PDB: 1Z8G), where the deviation between the Cα back bone of model and template was found as 0.33Å ( Figure 1E ;F). All three domains, LDL-receptor class A, SRCR and peptidase S1, formed distinct structural units in the molecular model. N-terminal region and LDL-receptor class A of TMPRSS2 were found more or less unstructured ( Figure 1G ;H).
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