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_9
Snippet: Human TMPRSS2 is 492 amino acid long protein with three functional domains: an N-terminal LDL-receptor class A domain (113-148) followed by SRCR (153-246) and finally at C-terminal peptidase S1 domain spanning from 256 to 487 amino acid ( Figure 1A) . Till now molecular structure of the protein has not been resolved and our XtalPred analysis showed the least possibility for this molecule to be crystalized, potentially due to the high percentage o.....
Document: Human TMPRSS2 is 492 amino acid long protein with three functional domains: an N-terminal LDL-receptor class A domain (113-148) followed by SRCR (153-246) and finally at C-terminal peptidase S1 domain spanning from 256 to 487 amino acid ( Figure 1A) . Till now molecular structure of the protein has not been resolved and our XtalPred analysis showed the least possibility for this molecule to be crystalized, potentially due to the high percentage of coiled structure, isoelectric point and surface hydrophobicity ( Figure 1B ). This may be the reason that Therefore, we used multiple approaches to develop the full length molecular model of TMPRSS2. The finally selected refined model of TMPRSS2 has 96.32% residues within the allowed regions of Ramachandran plot, which is acceptable considering the N-terminal portion of the protein was predicted to be intrinsically disordered. Secondly, it has been demonstrated rather frequently that many of the resolved structures of the proteins such as USP7 (PDB id: 2F1Z) have more than 20% of the residues outside the allowed region in Ramachandran plot. author/funder. All rights reserved. No reuse allowed without permission.
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