Unknown

Dataset Information

0

Structural and functional properties of SARS-CoV-2 spike protein: potential antivirus drug development for COVID-19.


ABSTRACT: Coronavirus disease 2019 is a newly emerging infectious disease currently spreading across the world. It is caused by a novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The spike (S) protein of SARS-CoV-2, which plays a key role in the receptor recognition and cell membrane fusion process, is composed of two subunits, S1 and S2. The S1 subunit contains a receptor-binding domain that recognizes and binds to the host receptor angiotensin-converting enzyme 2, while the S2 subunit mediates viral cell membrane fusion by forming a six-helical bundle via the two-heptad repeat domain. In this review, we highlight recent research advance in the structure, function and development of antivirus drugs targeting the S protein.

SUBMITTER: Huang Y 

PROVIDER: S-EPMC7396720 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural and functional properties of SARS-CoV-2 spike protein: potential antivirus drug development for COVID-19.

Huang Yuan Y   Yang Chan C   Xu Xin-Feng XF   Xu Wei W   Liu Shu-Wen SW  

Acta pharmacologica Sinica 20200803 9


Coronavirus disease 2019 is a newly emerging infectious disease currently spreading across the world. It is caused by a novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The spike (S) protein of SARS-CoV-2, which plays a key role in the receptor recognition and cell membrane fusion process, is composed of two subunits, S1 and S2. The S1 subunit contains a receptor-binding domain that recognizes and binds to the host receptor angiotensin-converting enzyme 2, while t  ...[more]

Similar Datasets

| EMPIAR-10999 | biostudies-other
| S-EPMC8995406 | biostudies-literature
| S-EPMC9961907 | biostudies-literature
| EMPIAR-10947 | biostudies-other
| S-EPMC7550470 | biostudies-literature
| S-EPMC7492024 | biostudies-literature
| S-EPMC7337374 | biostudies-literature
| S-EPMC7919520 | biostudies-literature
| S-EPMC8824715 | biostudies-literature
| S-EPMC8829538 | biostudies-literature