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SARS-CoV-2 proteins (version 2020.2) in the IUPHAR/BPS Guide to Pharmacology Database
Author(s) -
Stephen P.H. Alexander,
Jonathan K. Ball,
Theocharis Tsoleridis
Publication year - 2020
Publication title -
iuphar/bps guide to pharmacology cite
Language(s) - English
Resource type - Journals
ISSN - 2633-1020
DOI - 10.2218/gtopdb/f1034/2020.2
Subject(s) - transmembrane protein , biology , viral entry , genome , rna , polyproteins , viral structural protein , viral envelope , coronavirus , transmembrane domain , membrane protein , viral protein , viral replication , computational biology , virus , gene , virology , genetics , receptor , membrane , medicine , disease , covid-19 , pathology , infectious disease (medical specialty)
Coronaviruses are large, often spherical, enveloped, single-stranded positive-sense RNA viruses, ranging in size from 80-220 nm. Of the four structural proteins encoded in the viral genome, the RNA winds around the highly basic nucleocapsid (N) protein. The three other structural proteins, envelope (E), membrane (M) and spike (S), are transmembrane proteins. The E protein is a small (9-12 kDa) single transmembrane domain protein, which enables virus assembly with the M protein, a larger (23-35 kDa) 3TM protein. Coronaviruses are named for the crown-shaped appearance of the virus due to the large (120+ kDa) S spike 1TM glycoprotein, which forms extended homotrimers. The spike protein binds to the animal host cell by interacting with specific anchoring proteins, typically proteinases, such as angiotensin-converting enzyme 2 or aminopeptidase N. This binding facilitates viral entry into the cell and the release of the genome. Aside from the four structural proteins, the remainder of the genome encodes accessory or non-structural proteins and includes proteinases to cleave the two encoded polyproteins. The remainder of the genome encodes elements for viral replication, assembly and release, as well as proteins which manipulate the host's innate immune system.

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