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. 2022 Jun 17;30(9):1224–1232.e5. doi: 10.1016/j.str.2022.05.020

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The ET domain of BRD4 is an additional target of SARS-CoV-2 E

(A) The SARS-CoV-2 E peptides tested.

(B) Overlayed ¹H,¹⁵N HSQC spectra of the ¹⁵N-labeled BRD4 ET domain recorded before and after gradual addition of the indicated SARS-CoV-2 E peptides. The spectra are color-coded according to the protein:peptide molar ratio.

(C) Representative MST binding curves for the interaction of the BRD4 ET domain with the FAM-SARS-CoV-2 E^55-66 peptide. Data are representative of two experiments, and error represents SEM.

(D and E) Analysis of CSPs in the BRD4 ET domain induced by SARS-CoV-2 E^55-66. Residues of the BRD4 ET domain that exhibited large chemical shift perturbations (greater than the average plus 1 SD) upon addition of SARS-CoV-2 E^55-66 are mapped onto the BRD4 ET structure (2JNS), labeled, and colored orange in (D). Histogram of normalized CSPs in ¹H,¹⁵N HSQC spectra of BRD4 ET induced by 10-fold molar excess of SARS-CoV-2 E^55-66 as a function of residue is shown in (E). The dotted line indicates average chemical shift change plus 1 SD. Side chain amide resonances are indicated by asterisk.