Protein Surface Printer for Exploring Protein Domains.
J Chem Inf Model
; 60(10): 5255-5264, 2020 10 26.
Article
in English
| MEDLINE | ID: covidwho-733547
ABSTRACT
The surface of proteins is vital in determining protein functions. Herein, a program, Protein Surface Printer (PSP), is built that performs multiple functions in quantifying protein surface domains. Two proteins, PETase and cytochrome P450, are used to validate that the program supports atomistic simulations with different combinations of programs and force fields. A case study is conducted on the structural analysis of the spike proteins of SARS-CoV-2 and SARS-CoV and the human cell receptor ACE2. Although the surface domains of both spike proteins are highly similar, their receptor-binding domains (RBDs) and the O-linked glycan domains are structurally different. The O-linked glycan domain of SARS-CoV-2 is highly positively charged, which may promote binding to negatively charged human cells.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Software
/
Peptidyl-Dipeptidase A
/
Severe acute respiratory syndrome-related coronavirus
/
Spike Glycoprotein, Coronavirus
/
Betacoronavirus
Type of study:
Prognostic study
Limits:
Humans
Language:
English
Journal:
J Chem Inf Model
Journal subject:
Medical Informatics
/
Chemistry
Year:
2020
Document Type:
Article
Affiliation country:
Acs.jcim.0c00582
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