Hsp90 is an essential molecular chaperone responsible for the folding and activation of hundreds of ‘client’ proteins, including the glucocorticoid receptor (GR). Previously, we revealed that Hsp70 and Hsp90 remodel the conformation of GR to regulate l
Results A DNA primase-polymerase nonspecific of A or Z Parsing the genomic sequence of cyanophage S-2L (AX955019) in the search for a protein involved in DNA replication, we identified one ORF corresponding to a member of the Archaeo-Eukaryotic Primase (AEP) superfamily, which had not been...
This study has analyzed the presence of a furin-like cleavage site in the S protein of recently emerged coronaviruses, SARS-CoV-2, SARS-CoV, and MERS-CoV, using the Clustal omega tool. The results confirmed its absence in SARS-CoV and its presence in the other two coronaviruses (Fig. ...
The broadly neutralizing VRC34.01 branch required the rare heavy-chain mutation Y33P to bind FP, whereas the early bifurcated VRC34.05 branch did not require this rare mutation and evolved less breadth. Our results demonstrate how a required rare mutation can restrict development and shape the ...
results in a small increase in ligand binding but does not fully rescue ligand binding activity (Fig.3f). We reasoned this could be due to the inability of FKBP52 to sufficiently stabilize Hsp90 closure, as previously suggested53. Therefore, we added molybdate to these reactions, which ...