Literature summary for 3.4.21.B60 extracted from

Salleh, M.Z.; Deris, Z.Z.
In silico molecular characterization of human TMPRSS2 protease polymorphic variants and associated SARS-CoV-2 susceptibility (2022), Life, 12, 231 .

Search for more literature for 3.4.21.B60

Crystallization (Commentary)

Crystallization (Comment)	Organism
in silico binding analysis and molecular docking between TMPRSS2 and SARS-CoV-2 spike protein. TMPRSS2 binds in close proximity to two cleavage sites of the spike glycoprotein. Inhibitor camostat mesylate binds to the central cleft of TMPRSS2 via hydrogen bonding interactions with the residues C281, C297, V280, S436, W461 and G462. Inhibitor nafamostat forms 3 hydrogen bonds	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C297S	mutant is predicted to show altered interactions with the inhibitors, camostat mesylate and nafamostat	Homo sapiens
G462D	variant is predicted to be less susceptible to the SARS-CoV-2 infection and to show altered interactions with the inhibitors, camostat mesylate and nafamostat	Homo sapiens
G462S	variant is predicted to be less susceptible to the SARS-CoV-2 infection	Homo sapiens
Q438E	mutation is predicted to increase susceptibility to the SARS-CoV-2 infection	Homo sapiens
S339F	mutation is predicted to increase susceptibility to the SARS-CoV-2 infection	Homo sapiens
S460R	mutant is predicted to show altered interactions with the inhibitors, camostat mesylate and nafamostat	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
camostat mesylate	-	Homo sapiens
Nafamostat	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O15393	-	-

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Release 2023.1 (January 2023)