Figure 6b

OPEN and CLOSED state of SPIKE SARS-COV-2: relationship with some integrin binding. A biological molecular approach to better understand the coagulant effect

Luisetto M*, Khaled Edbey, Mashori GR, Yesvi AR and Latyschev OY

Published: 02 July, 2021 | Volume 5 - Issue 1 | Pages: 049-056

abb-aid1028-g006b

Figure 6b:

6b: Integrins, their ligands, and cellular distribution. According Hynes: integrins are organized in 24 different hetero-dimers, indicated by the link between α- and β-subunits in the figure. Integrins can be classified by structural -features, their ligands, and their tissue and cellular- expression. Based on these criteria, we grouped integrins into 9 classes indicated by the color of their background. Typical cell types expressing the respective integrins are mentioned, like common ligands for these integrins. We also highlighted integrins with an α-I domain (I; purple circle), those binding to RGD- ligands (RGD; red square), and those with changes to the conserved GFFKR sequence in the membrane-proximal part of the α-subunit (black triangle indicates integrins with sequence deviating from CGFFKR). The integrin- cartoon in the bottom part of the figure gives an overview about the integrin -structure and is reused in the following figures. It also indicates the location of the αI domain and the GFFKR sequence in the respective integrins. Please note that α-I domain integrins bind ligands (collagen) via this I domain, while other integrins bind ligands (fibronectin) in binding -pockets formed by both α- and β-subunits. Qiao B, de la Cruz MO. Enhanced Binding of SARS-CoV-2 Spike Protein to Receptor by Distal Polybasic Cleavage Sites. ACS Nano. 2020; 14: 10616–10623. https://doi.org/10.1021/acsnano.0c04798

Read Full Article HTML DOI: 10.29328/journal.abb.1001028 Cite this Article Read Full Article PDF

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