Author(s)
Gaetano T. Montelione
Published 3 Projects
Microbiology Bioinformatics Running Title Cell Division Divisome
Gaetano Montelione
Published 2 Projects
COVID-19 Microbiology Biochemistry Key Words Sars Cov 2 Pl Protease
Content
Video Abstract (AI generated) (01:48) Paper PreprintThe extra-terminal (ET) domain of BRD3 is conserved among BET proteins (BRD2, BRD3, BRD4), interacting with multiple host and viral protein-protein networks. Solution NMR structures of complexes formed between BRD3-ET domain with either the 79-residue murine leukemia virus integrase (IN) C-terminal domain (IN329-408), or its 22-residue IN tail peptide (TP) (IN386-407) alone, reveal similar intermolecular three-stranded β-sheet formation. 15N relaxation studies reveal a 10-residue linker region (IN379-388) tethering the SH3 domain (IN329-378) to the ET-binding motif (IN389-405)-ET complex. This linker has restricted flexibility, impacting its potential range of orientations in the IN - nucleosome complex. The complex of the ET-binding peptide of host NSD3 protein (NSD3148-184) and BRD3-ET domain includes a similar three-stranded β-sheet interaction, but the orientation of the β−hairpin is flipped compared to the two IN : ET complexes. These studies expand our understanding of molecular recognition polymorphism in complexes of ET-binding motifs with viral and host proteins. Highlights Etoc Blurb We address structurally how the MLV Integrase (IN) usurps the host function of the BET protein through comparative studies of the IN : Brd3 ET complex with that of the host NSD3. MLV integration and thus its pathogenesis is driven through protein interactions of the IN : BET family. ### Competing Interest Statement GL is an officer of Nexomics Biosciences, Inc. GTM is a founder of Nexomics Biosciences, Inc. These relationships do not present competing interests with respect to this paper.
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Gaetano Montelione. (2021, Nov 2).A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins[Video]. Scitok. https://scitok.com/project/p/387ea88b
Aiyer Sriram. "A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins" Scitok, uploaded by Montelione Gaetano, 2 Nov, 2021, https://scitok.com/project/p387ea88b
Gaetano Montelione. "A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins" Scitok. (Nov 2, 2021). https://scitok.com/project/p/387ea88b
Gaetano Montelione (Nov 2, 2021). A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins Scitok. https://scitok.com/project/p/387ea88b
Gaetano Montelione. A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins[video]. 2021 Nov 2. https://scitok.com/project/p/387ea88b
@online{al2006link, title={ A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins }, author={ Montelione, Gaetano }, organization={Scitok}, month={ Nov }, day={ 2 }, year={ 2021 }, url = {https://scitok.com/project/p/387ea88b}, }