Selected article for: "cell membrane and fusion protein"

Author: Erik Procko
Title: The sequence of human ACE2 is suboptimal for binding the S spike protein of SARS coronavirus 2
  • Document date: 2020_3_17
  • ID: jalijjmg_4
    Snippet: The S spike glycoprotein of SARS-CoV-2 binds angiotensin-converting enzyme 2 (ACE2) on 30 host cells (2, 8-13). S is a trimeric class I viral fusion protein that is proteolytically 31 processed into S1 and S2 subunits that remain noncovalently associated in a prefusion 32 state (8, 11, 14) . Upon engagement of ACE2 by a receptor binding domain (RBD) in S1 (15), 33 conformational rearrangements occur that cause S1 shedding, cleavage of S2 by host .....
    Document: The S spike glycoprotein of SARS-CoV-2 binds angiotensin-converting enzyme 2 (ACE2) on 30 host cells (2, 8-13). S is a trimeric class I viral fusion protein that is proteolytically 31 processed into S1 and S2 subunits that remain noncovalently associated in a prefusion 32 state (8, 11, 14) . Upon engagement of ACE2 by a receptor binding domain (RBD) in S1 (15), 33 conformational rearrangements occur that cause S1 shedding, cleavage of S2 by host 34 proteases, and exposure of a fusion peptide adjacent to the S2' proteolysis site (14, (16) (17) (18) . 35 Favorable folding of S to a post-fusion conformation is coupled to host cell/virus 36 membrane fusion and cytosolic release of viral RNA. Atomic contacts with the RBD are 37

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